2ped
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(New page: 200px<br /><applet load="2ped" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ped, resolution 2.95Å" /> '''Crystallographic mod...)
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Revision as of 10:36, 23 January 2008
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Crystallographic model of 9-cis-rhodopsin
Overview
The primary photochemical process of the visual function has been, investigated using the three crystallographic models, 11-cis-rhodopsin, all-trans-bathorhodopsin, and the artificial isomeric 9-cis-rhodopsin., Detailed examination of the atomic displacements and dihedral angle, changes of the retinal chromophore involved in the interconversion among, these isomers suggests the mechanism of isomerization efficiency.
About this Structure
2PED is a Single protein structure of sequence from Bos taurus with , , , , , and as ligands. Full crystallographic information is available from OCA.
Reference
Photoisomerization mechanism of rhodopsin and 9-cis-rhodopsin revealed by x-ray crystallography., Nakamichi H, Buss V, Okada T, Biophys J. 2007 Jun 15;92(12):L106-8. Epub 2007 Apr 20. PMID:17449675
Page seeded by OCA on Wed Jan 23 12:36:53 2008
Categories: Bos taurus | Single protein | Nakamichi, H. | Okada, T. | ACE | HG | HTG | HTO | PLM | RET | ZN | G protein-coupled receptor | Rhodopsin | Signaling protein | Visual pigment
