Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

G-protein coupled receptor structure.

Philip L Yeagle1, Arlene D Albert

  • 1Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269, USA. yeagle@uconn.edu

Biochimica Et Biophysica Acta
|November 14, 2006
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Unraveling a mystery: Why human cells require cholesterol.

Science advances·2022
Same author

Non-covalent binding of membrane lipids to membrane proteins.

Biochimica et biophysica acta·2013
Same author

A detergent-free strategy for the reconstitution of active enzyme complexes from native biological membranes into nanoscale discs.

BMC biotechnology·2013
Same author

Aggregatibacter actinomycetemcomitans leukotoxin cytotoxicity occurs through bilayer destabilization.

Cellular microbiology·2012
Same author

The bilayer enhances rhodopsin kinetic stability in bovine rod outer segment disk membranes.

Biophysical journal·2011
Same author

Assessment of bovine rod outer segment disk membrane heterogeneity utilizing flow cytometry.

Experimental eye research·2010
Same journal

Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Molecular Basis of Disease Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

General Subjects Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Erratum to 'on the role of exchangeable hydrogen bonds for the kinetics of P680<sup>+·</sup> Q<sub>A</sub> <sup>-·</sup> formation and P680<sup>+·</sup> Pheo<sup>-·</sup> recombination in photosystem II' [Biochim. Biophys. Acta 1276 (1996) 35-44].

Biochimica et biophysica acta·2019
Same journal

Oligomeric state of the light-harvesting complexes B800-850 and B875 from purple bacterium Rubrivivax gelatinosus in detergent solution.

Biochimica et biophysica acta·2019
Same journal

Regulation of pigment content and enzyme activity in the cyanobacterium Nostoc sp. Mac grown in continuous light, a light-dark photoperiod, or darkness.

Biochimica et biophysica acta·2019
See all related articles

Structure/function relationships for G-protein coupled receptors (GPCRs) are crucial for cellular regulation. While some structural data exist, more research is needed to fully understand GPCR activation mechanisms.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • G-protein coupled receptors (GPCRs) are vital for cellular function, regulating senses and intracellular signaling.
  • GPCRs are implicated in numerous diseases, highlighting the need for structural information.
  • Understanding GPCR structure is key to elucidating receptor action and regulation mechanisms.

Purpose of the Study:

  • To review the current state of knowledge regarding GPCR structure/function relationships.
  • To consolidate structural information obtained through various methods, including X-ray crystallography and non-crystallographic approaches.
  • To identify gaps in knowledge, particularly concerning GPCR activation and excited states.

Main Methods:

  • Review of existing literature on GPCR structural information, focusing on rhodopsin.

Related Experiment Videos

  • Analysis of X-ray crystallographic data, including bovine rhodopsin as the sole high-resolution example.
  • Inclusion of data from non-crystallographic methods for determining three-dimensional structures.
  • Examination of structural information related to ligand binding and receptor excited states.

    • Main Results:

    • The review covers early GPCR structural data, primarily from rhodopsin.
    • X-ray crystallography has yielded high-resolution structures for bovine rhodopsin, the only GPCR structure to date.
    • Non-crystallographic methods have provided considerable structural insights for various GPCRs.
    • Information on ligand binding and limited data on receptor excited states are also presented.

    Conclusions:

    • Significant progress has been made in obtaining basic structural information for GPCRs.
    • The available structural data, while valuable, are insufficient to fully describe the molecular mechanism of GPCR activation.
    • Further research is required to achieve a comprehensive understanding of GPCR function and regulation.