2i37
From Proteopedia
(New page: 200px<br /><applet load="2i37" size="450" color="white" frame="true" align="right" spinBox="true" caption="2i37, resolution 4.150Å" /> '''Crystal structure o...) |
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| - | [[Image:2i37.gif|left|200px]]<br /><applet load="2i37" size=" | + | [[Image:2i37.gif|left|200px]]<br /><applet load="2i37" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2i37, resolution 4.150Å" /> | caption="2i37, resolution 4.150Å" /> | ||
'''Crystal structure of a photoactivated rhodopsin'''<br /> | '''Crystal structure of a photoactivated rhodopsin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The changes that lead to activation of G protein-coupled receptors have | + | 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 Structure== | ==About this Structure== | ||
| - | 2I37 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with ACE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2I37 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I37 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Lodowski, D | + | [[Category: Lodowski, D T.]] |
[[Category: Palczewski, K.]] | [[Category: Palczewski, K.]] | ||
[[Category: Salom, D.]] | [[Category: Salom, D.]] | ||
| - | [[Category: Stenkamp, R | + | [[Category: Stenkamp, R E.]] |
| - | [[Category: Trong, I | + | [[Category: Trong, I Le.]] |
[[Category: ACE]] | [[Category: ACE]] | ||
[[Category: gpcr]] | [[Category: gpcr]] | ||
[[Category: trans-membrane protein]] | [[Category: trans-membrane protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:48:34 2008'' |
Revision as of 15:48, 21 February 2008
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Crystal structure of a photoactivated rhodopsin
Overview
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 Structure
2I37 is a Single protein structure of sequence from Bos taurus with as ligand. Full crystallographic information is available from OCA.
Reference
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
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