Home > Publications database > One of the Ca(2+) binding sites of recoverin exclusively controls interaction with rhodopsin kinase > print |
001 | 136533 | ||
005 | 20210129211846.0 | ||
024 | 7 | _ | |a 10.1515/BC.2005.034 |2 DOI |
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100 | 1 | _ | |a Komolov, K. E. |0 P:(DE-HGF)0 |b 0 |e Corresponding author |
245 | _ | _ | |a One of the Ca(2+) binding sites of recoverin exclusively controls interaction with rhodopsin kinase |
260 | _ | _ | |a Berlin [u.a.] |c 2005 |b de Gruyter |
336 | 7 | _ | |a article |2 DRIVER |
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336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1374675177_27988 |2 PUB:(DE-HGF) |
336 | 7 | _ | |a ARTICLE |2 BibTeX |
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336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
520 | _ | _ | |a Recoverin is a neuronal calcium sensor protein that controls the activity of rhodopsin kinase in a Ca(2+)-dependent manner. Mutations in the EF-hand Ca2+ binding sites are valuable tools for investigating the functional properties of recoverin. In the recoverin mutant E121Q (Rec E121Q ) the high-affinity Ca2+ binding site is disabled. The non-myristoylated form of Rec E121Q binds one Ca2+ via its second Ca(2+)-binding site (EF-hand 2), whereas the myristoylated variant does not bind Ca2+ at all. Binding of Ca2+ to non-myristoylated Rec E121Q apparently triggers exposure of apolar side chains, allowing for association with hydrophobic matrices. Likewise, an interaction surface for the recoverin target rhodopsin kinase is constituted upon Ca2+ binding to the non-acylated mutant. Structural changes resulting from Ca(2+)-occupation of EF-hand 2 in myristoylated and non-myristoylated recoverin variants are discussed in terms of critical conditions required for biological activity. |
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700 | 1 | _ | |a Zinchenko, D. V. |0 P:(DE-HGF)0 |b 1 |
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700 | 1 | _ | |a Senin, I. I. |0 P:(DE-HGF)0 |b 5 |
700 | 1 | _ | |a Philippov, P. P. |0 P:(DE-HGF)0 |b 6 |
700 | 1 | _ | |a Koch, K. W. |0 P:(DE-HGF)0 |b 7 |
773 | _ | _ | |0 PERI:(DE-600)1466062-3 |v 386 |t Biological chemistry |p 285-286 |x 1431-6730 |
856 | 4 | _ | |u http://www.ncbi.nlm.nih.gov/pubmed/15843174 |
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