%0 Journal Article
%A Komolov, K. E.
%A Zinchenko, D. V.
%A Churumova, V. A.
%A Vaganova, S. A.
%A Weiergräber, Oliver H.
%A Senin, I. I.
%A Philippov, P. P.
%A Koch, K. W.
%T One of the Ca(2+) binding sites of recoverin exclusively controls interaction with rhodopsin kinase
%J Biological chemistry
%V 386
%@ 1431-6730
%C Berlin [u.a.]
%I de Gruyter
%M FZJ-2013-03329
%P 285-286
%D 2005
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000228131400011
%R 10.1515/BC.2005.034
%U https://juser.fz-juelich.de/record/136533