2i94
From Proteopedia
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[[Image:2i94.gif|left|200px]] | [[Image:2i94.gif|left|200px]] | ||
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| - | | | + | {{STRUCTURE_2i94| PDB=2i94 | SCENE= }} |
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'''NMR Structure of recoverin bound to rhodopsin kinase''' | '''NMR Structure of recoverin bound to rhodopsin kinase''' | ||
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[[Category: Rhodopsin kinase]] | [[Category: Rhodopsin kinase]] | ||
[[Category: Ames, J B.]] | [[Category: Ames, J B.]] | ||
| - | [[Category: | + | [[Category: Calcium]] |
| - | [[Category: | + | [[Category: Ef-hand]] |
| - | [[Category: | + | [[Category: Phototransduction and rhodopsin kinse]] |
| - | [[Category: | + | [[Category: Recoverin]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:12:50 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 04:12, 4 May 2008
NMR Structure of recoverin bound to rhodopsin kinase
Overview
Recoverin, a member of the neuronal calcium sensor branch of the EF-hand superfamily, serves as a calcium sensor that regulates rhodopsin kinase (RK) activity in retinal rod cells. We report here the NMR structure of Ca(2+)-bound recoverin bound to a functional N-terminal fragment of rhodopsin kinase (residues 1-25, called RK25). The overall main-chain structure of recoverin in the complex is similar to structures of Ca(2+)-bound recoverin in the absence of target (<1.8A root-mean-square deviation). The first eight residues of recoverin at the N terminus are solvent-exposed, enabling the N-terminal myristoyl group to interact with target membranes, and Ca(2+) is bound at the second and third EF-hands of the protein. RK25 in the complex forms an amphipathic helix (residues 4-16). The hydrophobic face of the RK25 helix (Val-9, Val-10, Ala-11, Ala-14, and Phe-15) interacts with an exposed hydrophobic groove on the surface of recoverin lined by side-chain atoms of Trp-31, Phe-35, Phe-49, Ile-52, Tyr-53, Phe-56, Phe-57, Tyr-86, and Leu-90. Residues of recoverin that contact RK25 are highly conserved, suggesting a similar target binding site structure in all neuronal calcium sensor proteins. Site-specific mutagenesis and deletion analysis confirm that the hydrophobic residues at the interface are necessary and sufficient for binding. The recoverin-RK25 complex exhibits Ca(2+)-induced binding to rhodopsin immobilized on concanavalin-A resin. We propose that Ca(2+)-bound recoverin is bound between rhodopsin and RK in a ternary complex on rod outer segment disk membranes, thereby blocking RK interaction with rhodopsin at high Ca(2+).
About this Structure
2I94 is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
Reference
Structural basis for calcium-induced inhibition of rhodopsin kinase by recoverin., Ames JB, Levay K, Wingard JN, Lusin JD, Slepak VZ, J Biol Chem. 2006 Dec 1;281(48):37237-45. Epub 2006 Oct 4. PMID:17020884 Page seeded by OCA on Sun May 4 07:12:50 2008
