2i35: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2i35.gif|left|200px]] | [[Image:2i35.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_2i35", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
| | or leave the SCENE parameter empty for the default display. | ||
| | --> | ||
{{STRUCTURE_2i35| PDB=2i35 | SCENE= }} | |||
}} | |||
'''Crystal structure of rhombohedral crystal form of ground-state rhodopsin''' | '''Crystal structure of rhombohedral crystal form of ground-state rhodopsin''' | ||
| Line 30: | Line 27: | ||
[[Category: Stenkamp, R E.]] | [[Category: Stenkamp, R E.]] | ||
[[Category: Trong, I Le.]] | [[Category: Trong, I Le.]] | ||
[[Category: | [[Category: Trans-membrane protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:00:52 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 07:00, 4 May 2008
Crystal structure of rhombohedral crystal form of ground-state rhodopsin
OverviewOverview
The changes that lead to activation of G protein-coupled receptors have not been elucidated at the structural level. In this work we report the crystal structures of both ground state and a photoactivated deprotonated intermediate of bovine rhodopsin at a resolution of 4.15 A. In the photoactivated state, the Schiff base linking the chromophore and Lys-296 becomes deprotonated, reminiscent of the G protein-activating state, metarhodopsin II. The structures reveal that the changes that accompany photoactivation are smaller than previously predicted for the metarhodopsin II state and include changes on the cytoplasmic surface of rhodopsin that possibly enable the coupling to its cognate G protein, transducin. Furthermore, rhodopsin forms a potentially physiologically relevant dimer interface that involves helices I, II, and 8, and when taken with the prior work that implicates helices IV and V as the physiological dimer interface may account for one of the interfaces of the oligomeric structure of rhodopsin seen in the membrane by atomic force microscopy. The activation and oligomerization models likely extend to the majority of other G protein-coupled receptors.
About this StructureAbout this Structure
2I35 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a photoactivated deprotonated intermediate of rhodopsin., Salom D, Lodowski DT, Stenkamp RE, Le Trong I, Golczak M, Jastrzebska B, Harris T, Ballesteros JA, Palczewski K, Proc Natl Acad Sci U S A. 2006 Oct 31;103(44):16123-8. Epub 2006 Oct 23. PMID:17060607 Page seeded by OCA on Sun May 4 07:00:52 2008