2hpy

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Crystallographic model of lumirhodopsin

Overview

Photoactivation of the visual rhodopsin, a prototypical G protein-coupled, receptor (GPCR), involves efficient conversion of the intrinsic, inverse-agonist 11-cis-retinal to the all-trans agonist. This event leads, to the rearrangement of the heptahelical transmembrane bundle, which is, thought to be shared by hundreds of GPCRs. To examine this activation, mechanism, we determined the x-ray crystallographic model of the, photoreaction intermediate of rhodopsin, lumirhodopsin, which represents, the conformational state having the nearly complete all-trans agonist form, of the retinal. A difference electron density map clearly indicated that, the distorted all-trans-retinal in the precedent intermediate, bathorhodopsin relaxes by dislocation of the beta-ionone ring in, lumirhodopsin, along with significant peptide displacement in the middle, of helix III, including approximately two helical turns. This local, movement results in the breaking of the electrostatic interhelical, restraints mediated by many of the conserved residues among rhodopsin-like, GPCRs, with consequent acquisition of full activity.

About this Structure

2HPY is a Single protein structure of sequence from Bos taurus with HG, ZN, ACE, RET, PLM, HTO and HTG as ligands. Full crystallographic information is available from OCA.

Reference

Local peptide movement in the photoreaction intermediate of rhodopsin., Nakamichi H, Okada T, Proc Natl Acad Sci U S A. 2006 Aug 22;103(34):12729-34. Epub 2006 Aug 14. PMID:16908857

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