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Related Concept Videos

G Protein-coupled Receptors01:15

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
Channel Rhodopsins01:11

Channel Rhodopsins

Most organisms use photoreceptors to sense and respond to light. Examples of photoreceptors include bacteriorhodopsins and bacteriophytochromes in some bacteria, phytochromes in plants, and rhodopsins in the photoreceptor cells of the vertebral retina. The light-sensitive property of these receptors is because of the bound chromophores, such as bilin in the phytochromes and retinal in the rhodopsins.
Rhodopsins belong to the family of cell surface proteins called G-protein coupled receptors,...
Transducer Mechanism: Nuclear Receptors01:31

Transducer Mechanism: Nuclear Receptors

Nuclear receptors, or NRs, are unique transcription factors that regulate gene transcription and affect the cellular pathways involved in reproduction, development, or metabolism. Their ability to be stimulated by small lipophilic ligands and control vital cellular processes makes them ideal drug targets. Nearly 10-15% of currently prescribed drugs target these receptors.
About 48 different soluble family members of nuclear receptors are identified that can be divided into two main classes:
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
The Two-State Receptor Model01:29

The Two-State Receptor Model

The two-state receptor model explains a drug's interaction with receptors, such as G protein-coupled receptors and ligand-gated ion channels, to induce or inhibit a biological response. When no natural ligands are present, a receptor exists in an equilibrium of inactive (Ri) and active (Ra) conformations. The inactive form does not produce a response, while the active form generates a basal effect known as constitutive activity.
The binding affinity of a drug determines its interaction with one...

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Updated: May 20, 2026

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
11:31

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

Published on: November 30, 2018

Ryanodine receptors: structure and function.

Filip Van Petegem1

  • 1Department of Biochemistry and Molecular Biology, Life Sciences Institute, University of British Columbia, Vancouver V6T 1Z3, Canada. filip.vanpetegem@gmail.com

The Journal of Biological Chemistry
|July 24, 2012
PubMed
Summary
This summary is machine-generated.

Ryanodine receptors (RyRs) are large calcium channels crucial for muscle function. Mutations in these critical ion channels are linked to serious muscle and heart conditions, with structural insights aiding understanding.

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Measuring G-protein-coupled Receptor Signaling via Radio-labeled GTP Binding
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Last Updated: May 20, 2026

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
11:31

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

Published on: November 30, 2018

Measuring G-protein-coupled Receptor Signaling via Radio-labeled GTP Binding
10:13

Measuring G-protein-coupled Receptor Signaling via Radio-labeled GTP Binding

Published on: June 9, 2017

Area of Science:

  • Biophysics
  • Molecular Biology
  • Physiology

Background:

  • Ryanodine receptors (RyRs) are massive ion channels controlling calcium release from the sarco/endoplasmic reticulum.
  • These channels are essential for muscle contraction and cardiac function.
  • Numerous mutations in RyRs are implicated in skeletal muscle disorders and cardiac arrhythmias.

Purpose of the Study:

  • To summarize the structural characteristics of Ryanodine receptors.
  • To highlight the role of calcium (Ca2+) as a physiological ligand for RyRs.
  • To discuss the implications of RyR mutations in disease.

Main Methods:

  • Analysis of high-resolution structural data of RyR domains.
  • Mapping disease-associated mutations onto the three-dimensional structure of RyRs.
  • Review of existing literature on RyR function and modulation.

Main Results:

  • RyRs form large, homotetrameric channels with a distinct mushroom-like structure.
  • Calcium (Ca2+) acts as a key physiological activator.
  • Over 300 known mutations can be localized to specific regions of the RyR structure.

Conclusions:

  • Structural insights into Ryanodine receptors are advancing our understanding of their function.
  • The localization of mutations provides a structural basis for RyR-associated diseases.
  • Further structural studies will aid in developing therapeutic strategies for RyR-related disorders.