1l9h

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{{STRUCTURE_1l9h| PDB=1l9h | SCENE= }}
{{STRUCTURE_1l9h| PDB=1l9h | SCENE= }}
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'''Crystal structure of bovine rhodopsin at 2.6 angstroms RESOLUTION'''
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===Crystal structure of bovine rhodopsin at 2.6 angstroms RESOLUTION===
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==Overview==
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Activation of G protein-coupled receptors (GPCRs) is triggered and regulated by structural rearrangement of the transmembrane heptahelical bundle containing a number of highly conserved residues. In rhodopsin, a prototypical GPCR, the helical bundle accommodates an intrinsic inverse-agonist 11-cis-retinal, which undergoes photo-isomerization to the all-trans form upon light absorption. Such a trigger by the chromophore corresponds to binding of a diffusible ligand to other GPCRs. Here we have explored the functional role of water molecules in the transmembrane region of bovine rhodopsin by using x-ray diffraction to 2.6 A. The structural model suggests that water molecules, which were observed in the vicinity of highly conserved residues and in the retinal pocket, regulate the activity of rhodopsin-like GPCRs and spectral tuning in visual pigments, respectively. To confirm the physiological relevance of the structural findings, we conducted single-crystal microspectrophotometry on rhodopsin packed in our three-dimensional crystals and show that its spectroscopic properties are similar to those previously found by using bovine rhodopsin in suspension or membrane environment.
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(as it appears on PubMed at http://www.pubmed.gov), where 11972040 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11972040}}
==About this Structure==
==About this Structure==
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[[Category: Photoreceptor]]
[[Category: Photoreceptor]]
[[Category: Retinal protein]]
[[Category: Retinal protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:41:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 12:01:30 2008''

Revision as of 09:01, 2 July 2008

Image:1l9h.png

Template:STRUCTURE 1l9h

Crystal structure of bovine rhodopsin at 2.6 angstroms RESOLUTION

Template:ABSTRACT PUBMED 11972040

About this Structure

1L9H is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography., Okada T, Fujiyoshi Y, Silow M, Navarro J, Landau EM, Shichida Y, Proc Natl Acad Sci U S A. 2002 Apr 30;99(9):5982-7. Epub 2002 Apr 23. PMID:11972040

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