Acknowledgement of country¹

The University of Western Australia acknowledges that its campus is situated on Noongar land, and that Noongar people remain the spiritual and cultural custodians of their land, and continue to practise their values, languages, beliefs and knowledge.

Artist: Dr Richard Barry Walley OAM

DENT3005: assessment breakdown²

Assessment #	Assessment Task	Weight %	Assessment Period/ date	Module assessed	Waiver
1	SAQ	50%	30/09/25 9AM – 11AM	General Medicine and Pharmacology: all lectures content	No
2	MCQ	50%	Main Campus: Semester 2 examination period	General Medicine and Pharmacology: all lectures content	No

Learning outcomes³

Broad

Explain the principles of drug delivery, drug metabolism, and associated pharmacological aspects as they relate to dental practice
Define the terms receptor, drug agonist, and drug antagonist
Describe the different types of receptor and pharmacodynamic factors influencing drug-receptor interactions

Specific topics we will cover:

Receptors
Drug-induced responses
Receptor agonist and antagonist
Possible drug targets
Four main drug receptors: Ion channels, G protein-coupled receptors, kinase-linked receptors, nuclear receptors

Pharmacodynamics vs. Pharmacokinetics⁴

Pharmacodynamics	Pharmacokinetics
Pharmacodynamics = What the DRUG does to the BODY	Pharmacokinetics = What the BODY does to the DRUG

Key terms⁵

Receptor
Affinity
Agonism
Antagonism
Competitive and noncompetitive enzyme inhibition
Efficacy
Potency
Receptors
Specificity

What is a drug?⁶

A chemical $\to$ produce biological effect

How are drugs classified?

Chemical structure
Mechanism of action- how does it work?
Therapeutic use – what is it designed to do?

Drug nomenclature

Chemical name
- Eg. 7,8-didehydro-4,5a-epoxy-17-methylmorphinan-3,6a-diol sulfate!!!!!
Generic name
- Eg. Morphine sulfate
Brand name
- Eg. Kapanol, Ms Contin, Ms Mono…

Basic principle⁷

Drug molecule exerting chemical influence $\to$ pharmacological response
Non-uniform distribution
Drug must be bound to a critical binding site “target”

Protein targets

Receptors
Enzymes
Carrier molecules (transporters)
Ion channels

How drugs function?

Agonist
Antagonist
Inverse agonist
Toxicity?

What is a receptor?⁸

Specialized proteins
On cell surfaces/within cells
Transmit signals in the body

Importance

Key players in mediating the effects of drugs
Cellular communication

Binding

ligand-receptor interaction

Signal transduction

ligand binding triggering cellular changes

Drug-receptor interactions:⁹

Chemical structure
Molecular size and shape
Lipophilicity
pH & lonization

Drug binding & receptor activation

Affinity
Efficacy

Drug-Receptor Binding¹⁰

Affinity

Tendency of a drug to bind to a receptor

$↑$ Affinity = Greater binding tendency
Measured by Kd (Equilibrium dissociation constant, mol/L)
Lower Kd = Higher affinity

Efficacy

Ability of a drug to produce an effect at the receptor

$↑$ Efficacy = Greater maximum effect
More efficacious drug = Greater effect, not necessarily stronger binding
Agonist: Has both affinity and efficacy
Antagonist: Has affinity, but no efficacy

$[D] + [R] k_{- 1} ⇌ k_{1} [D R]$ Reversible reaction

k $_1$ & k $_- 1$ are the rate constants for association and dissociation

$K_{D} = \frac{k _{- 1}}{k _{1}}$

Drugs with $↓$ Low Kd = $↑$ Affinity
Drugs with $↑$ High Kd = $↓$ Affinity

Drug-Receptor interactions, EKG Science

Drug-Receptor Binding¹⁰

Potency

(the relative amount of drug that has to be present to produce an effect)

EC $_{50}$ –the concentration at which 50% of the max response (to the drug) is observed
$↑$ EC $_{50}$ : more drug req = lower potency

Specificity

(relates to degree of selectivity)

$↑$ Specificity: targeted action, lowered side-effects

Fundamentals of Pharmacology

Drug-Receptor Binding¹⁰

Agonist

An agonist is a drug that binds to and activates a receptor

Partial agonist

can bind to and activate the receptor
Lower efficacy – cannot produce the same maximum effect as a full agonist

Antagonist

An antagonist is a drug that binds to the receptor & does NOT cause activation

Competitive antagonist: reversible/ surmountable
Non-competitive antagonist: irreversible/ insurmountable
Physiological antagonism: 2 drugs have effects that are functionally the opposite

RECAP Efficacy: The ability of the agonist- receptor complex to initiate changes that induce a response

Drug-Receptor interactions, EKG Science

flowchart TD
    subgraph Drug A Binding and Effect
        A["Drug A (agonist)"] --> B(R)
        B -- Affinity, k1 --> C(AR)
        B -- k-1 --> A
        C -- Efficacy, β --> D(AR*)
        C -- α --> B
        D --> E[Response]
    end
    subgraph Agonist Action
        Agonist[Agonist] --> Receptor1(Receptor)
        Receptor1 --> F[Full activation & Response]
    end

flowchart TD
    subgraph Drug B Binding and Effect
        G["Drug B (antagonist)"] --> H(R)
        H -- Affinity, k1 --> I(BR)
        H -- k-1 --> G
        I --> J[No Response]
    end
    subgraph Antagonist Action
        Antagonist[Antagonist] --> Receptor2(Receptor)
        Receptor2 --> K[No activation & response]
    end

Inverse Agonist¹¹

Inverse agonist are special
Pharmacological agonist
Decrease level of receptor activation
- Negative efficacy
NOT an antagonist
- Do not cause activation (zero efficacy)

Pharmacologic Agonists

Drug	Receptor	Effect
Full agonist
Partial agonist
Inverse agonist

Drug-Receptor Binding¹⁰

Concentration-response curves (CRC)

Tool for understanding the connection between a drug and its biological effects

Agonists

Emax – is the maximum response that can be achieved by the drug under the given conditions
EC50 – is the drug concentration at which 50% of the maximum response (to the drug) is observed
EC50 provides a measure of drug potency

RECAP Potency: measure of drug activity/ amount of drug that is required to produce a particular effect

Lower EC50 = Higher potency
Low potency – requires a higher concentration

Concentration-Response Curve Diagram

The image displays a graph illustrating a concentration-response curve (CRC) and associated concepts.

Y-axis: % response (from 0 to 100)
X-axis: [Agonist] (M) (from $1 0^{- 12}$ to $1 0^{- 2}$ )

Key labels on the graph:

Emax
Increased risk of adverse reactions
Therapeutic range
EC50
Sub-therapeutic effect

Drug-Receptor interactions, EKG Science

Drug-Receptor Binding¹⁰

Concentration-response curves (CRC) for Antagonists

Competitive Antagonist

Agonist and antagonist compete for the same Orthosteric site
Surmountable – increasing the con. of the agonist can overcome the binding of the competitive antagonist
Increasing con. of a competitive antagonist will cause a parallel rightward shift in the agonist CRC

Non-competitive antagonist

Insurmountable – antagonist drug reduces the maximum effect of the agonist
Irreversibly alters the target receptors (e.g. forming covalent bonds)
High affinity for the receptor- dissociates slowly.
Maximum response cannot be achieved

Lambert DG. (2004). Drugs and receptors. Continuing Education in Anaesthesia Critical Care & Pain; 4(6):181–184.

Other considerations¹²¹³

Drugs that work by simple chemical or physical action
- Neutralization of acidic environment
- Chelating
- Osmosis

Protein Targets for Drug Action¹⁴

subgraph B ION CHANNELS
    B1(Blockers) --> B1.1(Permeation blocked)
    B2(Modulators) --> B2.1(Increased or decreased opening probability)
end

subgraph C ENZYMES
    C1(Inhibitor) --> C1.1(Normal reaction inhibited)
    C2(False substrate) --> C2.1(Abnormal metabolite produced)
    C3(Prodrug) --> C3.1(Active drug produced)
end

subgraph D TRANSPORTERS
    D1(Normal transport) --> D1.1(Transported compound)
    D2(Inhibitor) --> D2.1(Transport blocked)
    D3(False substrate) --> D3.1(Abnormal compound accumulated)
end

Agonist/substrate

Antagonist/inhibitor

Abnormal product

Prodrug

Rang & Dale’s Pharmacology, Tenth Edition

Types of Receptors¹⁵

Receptor: Specialized proteins located on cell surfaces/within cells that are responsible for transmitting signals in the body

1. Ligand-gated ion channels (ionotropic receptors)	2. G protein-coupled receptors (metabotropic)	3. Kinase-linked receptors	4. Nuclear receptors

graph TD
    A[Ions] --> B{Hyperpolarisation or depolarisation};
    A --> C{Change in excitability};
    C --> D[Ca²⁺ release];
    R(R) --> E{Second messengers}
    E --> F[Protein phosphorylation];
    E --> G[Other];
    R/E(R/E) --> H[Protein phosphorylation];
    H --> I[Gene transcription];
    I --> J[Protein synthesis];
    N(NUCLEUS: R) --> K[Gene transcription];
    K --> L[Protein synthesis];
    B --> M[Cellular effects];
    D --> M;
    F --> M;
    G --> M;
    J --> M;
    L --> M;

    subgraph Time Scale
      style Time Scale fill:#f0f0f0

        Mmillisecond[Milliseconds]
        Ssecond[Seconds]
        Hhour[Hours]
        H2hour[Hours]
    end

    subgraph Examples
      style Examples fill:#f0f0f0

        N(Nicotinic ACh receptor)
        M2(Muscarinic ACh receptor)
        C(Cytokine receptors)
        O(Oestrogen receptor)
    end
    
    Mmillisecond --> N
    Ssecond --> M2
    Hhour --> C
    H2hour --> O

Time scale

Milliseconds	Seconds	Hours	Hours
Examples	Muscarinic ACh receptor	Cytokine receptors	Oestrogen receptor
Nicotinic ACh receptor

Rang & Dale’s Pharmacology, Tenth Edition

Types of Receptors: in a nutshell!¹⁶

	Type 1: Ligand gated ion channels	Type 2: G-Protein coupled receptors	Type 3: Receptor kinases	Type 4: Nuclear receptors
Location	Membrane	Membrane	Membrane	Intracellular
Effector	Ion Channel	Channel or enzyme	Protein Kinases	Genes Transcription
Coupling	Direct	G Protein or arrestin	Direct	Via DNA
Examples	Nicotinic acetylcholine receptor, GABAA receptor	Muscarinic acetylcholine receptors, adrenoceptors	Insulin, growth factors, cytokine receptors	Steroid receptors
Structure	Oligomeric assembly of subunits surround central pore	Monomeric/oligomeric assembly of subunits: 7 transmembrane helices with intracellular G-Protein coupling domain	Single transmembrane helix linking extracellular receptor domain to intracellular kinase domain	Monomeric structure with receptor and DNA binding domains

Rang & Dale’s Pharmacology, Tenth Edition

Type 1: Ligand-gated Ion Channel receptors¹⁷

Ionotropic
Neurotransmitters
Timescale: milliseconds
Localization: membrane
Effector: ion channel
Coupling: direct

Ion channels are characterized by

Selectivity for particular ion species

Size of the pore and nature of its lining
Cations: $N a^{+}$ , $C a^{2 +}$ , $K^{+}$
Anions: $Cl^{-}$

Gating properties

Control transition from open to closed states

Molecular structure

4-5 subunits

Examples

Nicotinic Ach Receptor
GABA A Receptor
Glutamate Receptor
Glycine Receptor

Types of receptors, EKG Science

Example: Nicotinic Acetylcholine Receptor¹⁸

Nicotine

Outside of cell
Cell membrane
Inside of cell

GABA

Outside of cell
Cell membrane
Inside of cell

Element	Description
ACH (ACh)	Acetylcholine binding site
$α$ , $β$ , $δ$ , $γ$	Receptor subunits
a-Helices forming gate	Structure controlling channel opening
Pore (~0.7 nm)	The opening for ion passage
Closed channel	Receptor state without ligand binding
Open channel	Receptor state after ligand binding (Nicotine or GABA)
$N a^{+}$	Sodium ion flow through nAChR
$C l^{-}$ , $K^{+}$	Chloride and Potassium ion flow through GABA receptor

Type 2: G-protein coupled receptors¹⁹²⁰

Metabotropic
Largest family
Timescale: seconds
Location: membrane
Effector: channel or enzyme
Coupling: G-Protein

Function

Recognise and activate GPCRs $\to$ pass message to effector system $\to$ generate cellular response
Signal amplification
Four main classes

Binding domains

Outside of cell
Cell membrane
Inside of cell

G-protein coupling domain

Examples

Adrenoceptors
Muscarinic Ach
Histamine
Serotonin
Opioid

Example: cyclic AMP pathways²¹²²

G-protein coupling domain comprises of 3 subunits ( $α$ , $β$ , $γ$ )
G $α$ proteins link GPCRs to effector proteins that generate intracellular second messengers
- G $α$ s - Activates adenylate cyclase- Generates cAMP
- G $α$ i- Inhibits adenylate cyclase
- G $α$ q - Activates phospholipase C- Generates inositol triphosphate and diacylglycerol

Adenylate cyclase signal transduction pathway

GTP binds to G $α$ $\to$ Activation of G protein
G $α$ dissociates from G $\beta$$\gamma$ $\to$ Binds to adenylate cyclase $\to$ activation of cAMP
G $α$ dissociates from adenylate cyclase $&$ binds to G $\beta$$\gamma$ $\to$ inactivation of cAMP
Returning to G state

graph TD
    A[Agonist] --> B(GPCR);
    B --> C{GTP};
    C --> D[Gα];
    C --> E[Gαs];
    C --> F[Gαi];
    C --> G[Gαq];
    D --> H[Gβγ];
    B --> H;

    E --> I[AC];
    F -.- I; % Inhibitory link shown by dashed line/red arrow in original figure/image
    I --> J[ATP];
    J --> K[cAMP];
    K --> L[PKA];
    
    G --> M[PLC];
    H --> N[Ion channel];
    N --> O(Ions);
    
    M --> P[PIP2];
    P --> Q[DAG];
    P --> R[IP3];
    Q --> S[PKC];
    R --> T[Ca2+ from ER lumen];
    S --> U[Ca2+];
    T --> U;
    
    D --> V[Gα 12/13];
    V --> W[RhoGEF];
    W --> X[RhoA];

style E fill:#4CAF50,stroke:#333
style F fill:#4CAF50,stroke:#333
style G fill:#4CAF50,stroke:#333
style V fill:#4CAF50,stroke:#333
style I fill:#FFCC80,stroke:#333
style M fill:#4D8EDD,stroke:#333
style L fill:#FF4D4D,stroke:#333
style S fill:#FF4D4D,stroke:#333
style W fill:#AAAAAA,stroke:#333
style X fill:#AAAAAA,stroke:#333
style Q fill:#FFCC80,stroke:#333
style R fill:#FFCC80,stroke:#333
style K fill:#FF4D4D,stroke:#333
style N fill:#FFCC80,stroke:#333

Chen Y, Palczewski K. (2016). Systems Pharmacology Links GPCRs with Retinal Degenerative Disorders. Annu Rev Pharmacol Toxicol;56:273-98.Rang & Dale’s Pharmacology, Ninth Edition

Rang & Dale’s Pharmacology, Tenth Edition

Gα subunits^b
Gα _s	Stimulates adenylyl cyclase, causing increased cAMP formation	Activated by cholera toxin, which blocks GTPase activity, thus preventing inactivation
Gα _i	Inhibits adenylyl cyclase, decreasing cAMP formation	Blocked by pertussis toxin, which prevents dissociation of αβγ complex
Gα _o	Limited effects of α subunit (effects mainly due to βγ subunits)	Blocked by pertussis toxin. Occurs mainly in nervous system
Gα _q	Activates phospholipase C, increasing production of second messengers inositol trisphosphate and diacylglycerol thus releasing Ca ²⁺ from intracellular stores and activating protein kinase C (PKC)
Gα _12/13	Activates Rho and thus Rho kinase
Gβγ subunits	Activate potassium channels Inhibit voltage-gated calcium channels Activate GPCR kinases (GRKs) Activate mitogen-activated protein kinase cascade Interact with some forms of adenylyl cyclase and with phospholipase Cβ	Many βγ isoforms identified, but specific functions are not yet known

Type 3: Kinase linked receptors²³²⁴²⁵

Large heterogenous group responding mainly to protein mediators

Time scale: hours
Location: membrane
Effector: protein kinases
Coupling: direct
Structure: single transmembrane helix- linking extracellular receptor domain to intracellular kinase domain

Receptor types

Receptor tyrosine kinase – growth factors, insulin and IGF (insulin-like growth factor)
Receptor serine/threonine kinase – transforming growth factor
Cytokine receptor – interleukins and interferons
Receptor guanylate cyclase – natriuretic peptides

Examples

Insulin
Growth Factors
Cytokine
ANF receptors

Receptor tyrosine kinase²⁶

Ras/Raf/MAP kinase pathway

Ligand binding
Receptor dimerises
Tyrosine autophosphorylation
Binding of SH2- domain protein (Grb2)
Kinase cascade (Raf, Mek, MAPkinase)
Transcription factor
Gene transcription

*Grb2- Growth factor receptor bound protein 2 (an adaptor protein); SH – Src homology

Rang & Dale’s Pharmacology, Tenth Edition

graph TD
    A[Growth factor] --> B{Receptor domain};
    B --> C[Conformation change / Dimerisation];
    C --> D[Tyrosine autophosphorylation];
    D --> E[Phosphorylation of Grb2 / Binding of SH2-domain protein (Grb2)];
    E --> F[Ras-GDP/GTP exchange Activation of Ras];
    F --> G[Raf];
    G --> H[Mek Phosphorylation];
    H --> I[MAP kinase Phosphorylation];
    I --> J[Various transcription factors Phosphorylation];
    J --> K[Gene transcription NUCLEUS];

    %% Other labels from the diagram
    subgraph Receptor
        B_receptor(Receptor domain);
        C_dimer(Dimerised receptor);
        D_phosph(Autophosphorylated receptor);
        E_grb2(Grb2 bound);
        B_receptor---Trans(Transmembrane $\alpha$ helix);
        B_receptor---TyrKinase(Tyrosine kinase domain);
        TyrKinase---TyrRes(Tyrosine residue);
    end

    subgraph KINASE CASCADE
        G;
        H;
        I;
    end

Receptor tyrosine kinase²⁶

Jak/stat pathway

graph TD
    A[Cytokine] --> B{Receptor}
    B -- Ligand binding --> C{Dimerisation<br>Conformation change<br>activation of Jak}
    C --> D{Phosphorylation of receptor<br>+ Jak}
    D -- Binding and phosphorylation of SH2-domain (Stat) --> E[Stat<br>SH2-domain protein]
    E --> F{Dimerisation of Stat}
    F --> G[Gene transcription<br>in NUCLEUS]
    D -- Location --> MEMBRANE

    subgraph Steps
        1(Ligand binding)
        2(Receptor dimerises)
        3(Phosphorylation of receptor and Jak)
        4(Binding of SH2- domain protein (Stat))
        5(Dimerization of Stat)
        6(Gene transcription)
    end

*JAK – Janus kinase; STAT – signal transducer and activator of activator of transcription Rang & Dale’s Pharmacology, Tenth Edition

Type 4: Nuclear receptors²⁷²⁸

Regulate gene transcription, metabolic and developmental processes Not always in the nucleus

Time scale: Hours
Location: intracellular
Effector: Gene transcription
Coupling: via DNA
Structure: monomeric proteins typically composed of several domains each with distinct functions
- N-terminal domain
- Core domain
- Hinge Region
- C-terminal domain

Examples

Steroid hormones
Thyroid hormones
Retinoic acid
Vitamin D receptors

Class I: Steroid Receptors (SR)	Class II: Retinoid X Receptor (RXR) Heterodimers

Glucocorticoid Mineralocorticoid Progesterone Estrogen	Thyroid hormone RAR $α$
Class III: Dimeric Orphan Receptors (DOR)	Class IV: Monomeric Orphan Receptors (MOR)

Type 4: Nuclear receptors²⁷²⁸

Steroid Receptors (Class I)

Steroid hormones are lipophilic and can easily enter cell membranes
Lipophilic ligands interact with nuclear receptors once inside the cell
Functional effects of nuclear receptors are slow due to their role in gene transcription and protein synthesis
In the absence of ligand, nuclear receptors are mostly in the cytoplasm, bound to heat shock proteins (HSPs)

graph TD
    subgraph Cell
        direction TB
        Outside_of_cell
        Cell_membrane
        Inside_of_cell
    end

    Steroid_hormone(Steroid hormone)
    Steroid_hormone --> Inside_of_cell

    Inside_of_cell --> Steroid_receptor_inactive(Steroid receptor)
    Steroid_hormone --> Hormone_receptor_complex_active(Hormone-receptor complex)
    Steroid_receptor_inactive --- Hormone_receptor_complex_active
    Hormone_receptor_complex_active --> Nucleus_membrane[Inside Nucleus]

    Nucleus_membrane --> Complex_binds_to_sites_on_DNA(Complex binds to sites on DNA)
    Complex_binds_to_sites_on_DNA --> Cellular_response(Cellular response)

Type 4: Nuclear receptors²⁷²⁸

Steroid Receptors (Class II)

Operate as heterodimers with RXR
Two types of heterodimers:
- Non-permissive: activated only by RXR ligand
- Permissive: activated by retinoic acid or partner ligand
Typically bound to co-repressor proteins to suppress gene expression
Ligand binding causes dissociation of co-repressors and recruitment of co-activators
Co-activator recruitment initiates gene expression

graph TD
    subgraph Nucleus
        M[Nucleus];
        C;
        D;
        E;
        F;
    end
    
    subgraph Cytoplasm
        K[Cytoplasm];
        L[Nuclear envelope];
    end

    A[Hormone] --> B(Nuclear pore);
    B --> C{Receptor Heterodimer with Corepressor (LBD: Ligand Binding Domain, DBD: DNA Binding Domain, RXR: Retinoid X Receptor, T/R: Thyroid/Retinoic Acid Receptor) bound to HRE on target gene};
    style C fill:#faa, stroke:#ff0000, color:#000000;
    A --> C;
    C --> D[Dissociation of Corepressor and Recruitment of Coactivator and RNA Polymerase];
    style D fill:#ddf, stroke:#00aa00, color:#000000;
    D --> E[Transcription of target gene: mRNA];
    D --> F[RNA Polymerase];
    E --> G(Nuclear pore);
    G --> H[Ribosome in Cytoplasm];
    H --> I[Protein synthesis];
    I --> J[Changed cell function];

Key information²⁹³⁰

Most drugs bind to, and act through receptors
Majority of drugs receptors are proteins
Four superfamilies of receptors are presented
Effects of drug after binding to a receptor is called signal transduction
Agonists at a given at a given receptor can be distinguished based upon affinity and efficacy
Antagonists are drugs that bind to receptors and block the effects of agonists

References³¹

Ritter JM, Flower RJ, Henderson G, Loke YK, MacEwan D, Robinson E, editors. Rang & Dale’s pharmacology. 10th ed. Edinburgh: Elsevier; 2023
Becker DE, Reed KL. Pharmacology and Therapeutics for Dentistry. 7th ed. St. Louis: Elsevier; 2017.
Bullock S, Manias E. Fundamentals of pharmacology. 8th ed. Frenchs Forest, NSW: Pearson Australia; 2017
Stringer JL. Basic concepts in pharmacology. 6th ed. New York (US): McGraw Hill Medical; 2022 Feb 18

Images of people suffering from illnesses and medication jars.

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Quartz 4

Explorer

L2 PHARMACODYNAMICS 2025_formatted_text

Acknowledgement of country1

DENT3005: assessment breakdown2

Learning outcomes3

Broad

Specific topics we will cover:

Pharmacodynamics vs. Pharmacokinetics4

Key terms5

What is a drug?6

How are drugs classified?

Drug nomenclature

Basic principle7

Protein targets

How drugs function?

What is a receptor?8

Importance

Binding

Signal transduction

Drug-receptor interactions:9

Drug binding & receptor activation

Drug-Receptor Binding10

Affinity

Efficacy

Drug-Receptor Binding10

Potency

Specificity

Drug-Receptor Binding10

Agonist

Partial agonist

Antagonist

Inverse Agonist11

Pharmacologic Agonists

Drug-Receptor Binding10

Concentration-response curves (CRC)

Agonists

Concentration-Response Curve Diagram

Drug-Receptor Binding10

Concentration-response curves (CRC) for Antagonists

Competitive Antagonist

Non-competitive antagonist

Other considerations1213

Protein Targets for Drug Action14

Types of Receptors15

Types of Receptors: in a nutshell!16

Type 1: Ligand-gated Ion Channel receptors17

Ion channels are characterized by

Examples

Example: Nicotinic Acetylcholine Receptor18

Type 2: G-protein coupled receptors1920

Function

Binding domains

G-protein coupling domain

Examples

Example: cyclic AMP pathways2122

Adenylate cyclase signal transduction pathway

Type 3: Kinase linked receptors232425

Receptor types

Examples

Receptor tyrosine kinase26

Ras/Raf/MAP kinase pathway

Receptor tyrosine kinase26

Jak/stat pathway

Type 4: Nuclear receptors2728

Examples

Type 4: Nuclear receptors2728

Steroid Receptors (Class I)

Type 4: Nuclear receptors2728

Steroid Receptors (Class II)

Key information2930

References31

Footnotes

Graph View

Table of Contents

Acknowledgement of country¹

DENT3005: assessment breakdown²

Learning outcomes³

Pharmacodynamics vs. Pharmacokinetics⁴

Key terms⁵

What is a drug?⁶

Basic principle⁷

What is a receptor?⁸

Drug-receptor interactions:⁹

Drug-Receptor Binding¹⁰

Drug-Receptor Binding¹⁰

Drug-Receptor Binding¹⁰

Inverse Agonist¹¹

Drug-Receptor Binding¹⁰

Drug-Receptor Binding¹⁰

Other considerations¹²¹³

Protein Targets for Drug Action¹⁴

Types of Receptors¹⁵

Types of Receptors: in a nutshell!¹⁶

Type 1: Ligand-gated Ion Channel receptors¹⁷

Example: Nicotinic Acetylcholine Receptor¹⁸

Type 2: G-protein coupled receptors¹⁹²⁰

Example: cyclic AMP pathways²¹²²

Type 3: Kinase linked receptors²³²⁴²⁵

Receptor tyrosine kinase²⁶

Receptor tyrosine kinase²⁶

Type 4: Nuclear receptors²⁷²⁸

Type 4: Nuclear receptors²⁷²⁸

Type 4: Nuclear receptors²⁷²⁸

Key information²⁹³⁰

References³¹