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Signal transmission via G protein-coupled receptors in the light of rhodopsin structure determination.
Author(s) -
Jerzy Ciarkowski,
Piotr Drabik,
Artur Giełdoń,
Rajmund Kaźmierkiewicz,
Rafał Ślusarz
Publication year - 2001
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.2001_3892
Subject(s) - g protein coupled receptor , heterotrimeric g protein , rhodopsin , g protein , receptor , chemistry , signal transduction , biophysics , microbiology and biotechnology , computational biology , biology , biochemistry , retinal
G protein-coupled receptors (GPCRs) transducing diverse external signals to cells via activation of heterotrimeric GTP-binding (G) proteins, estimated to mediate actions of 60% of drugs, had been resistant to structure determination until summer 2000. The first atomic-resolution experimental structure of a GPCR, that of dark (inactive) rhodopsin, thus provides a trustworthy 3D prototype for antagonist-bound forms of this huge family of proteins. In this work, our former theoretical GPCR models are evaluated against the new experimental template. Subsequently, a working hypothesis regarding the signal transduction mechanism by GPCRs is presented.

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