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Article

Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin.

Science (New York, N.Y.) - 1 Nov 1996

Farrens D L, Altenbach C, Yang K, Hubbell W L, Khorana H G

Abstract excerpt

Conformational changes are thought to underlie the activation of heterotrimeric GTP-binding protein (G protein)-coupled receptors. Such changes in rhodopsin were explored by construction of double cysteine mutants, each containing one cysteine at the cytoplasmic end of helix C and one cysteine at various positions in the cytoplasmic end of helix F. Magnetic dipolar interactions between spin labels attached to...

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Identifiers

PMID: 8864113
DOI: 10.1126/science.274.5288.768

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Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin.PMID 8864113Read ↗

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Intramolecular interactions that induce helical rearrangement upon rhodopsin activation: light-induced structural changes in metarhodopsin IIa probed by cysteine S-H stretching vibrations.Semantic proximity Read ↗

Highly conserved tyrosine stabilizes the active state of rhodopsin.Semantic proximity Read ↗

Dynamics of the Second Extracellular Loop Control Transducer Coupling of Peptide-Activated GPCRs.Semantic proximity Read ↗

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