001     136533
005     20210129211846.0
024 7 _ |a 10.1515/BC.2005.034
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037 _ _ |a FZJ-2013-03329
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100 1 _ |a Komolov, K. E.
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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
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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.
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700 1 _ |a Churumova, V. A.
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700 1 _ |a Vaganova, S. A.
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700 1 _ |a Weiergräber, Oliver H.
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700 1 _ |a Senin, I. I.
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700 1 _ |a Philippov, P. P.
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700 1 _ |a Koch, K. W.
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856 4 _ |u http://www.ncbi.nlm.nih.gov/pubmed/15843174
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