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| - | [[Image:2i94.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2i94| PDB=2i94 | SCENE= }} | | {{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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| - | ==Overview==
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| - | 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+).
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17020884}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17020884 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17020884}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 2I94 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I94 OCA]. | + | 2I94 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I94 OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Phototransduction and rhodopsin kinse]] | | [[Category: Phototransduction and rhodopsin kinse]] |
| | [[Category: Recoverin]] | | [[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 Mon Jul 28 08:32:25 2008'' |
Revision as of 05:32, 28 July 2008
Template:STRUCTURE 2i94
NMR Structure of recoverin bound to rhodopsin kinase
Template:ABSTRACT PUBMED 17020884
About this Structure
2I94 is a Protein complex structure of sequences from Bos taurus. Full experimental 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 Mon Jul 28 08:32:25 2008
