Calmodulin bridging of IQ motifs in myosin-V

被引：30
|
作者：
Martin, SR [1 ]
Bayley, PM [1 ]
机构：
[1] Natl Inst Med Res, Div Phys Biochem, London NW7 1AA, England
来源：
FEBS LETTERS | 2004年 / 567卷 / 2-3期
关键词：
calmodulin; IQ motif; myosin-V; motility; calcium regulation; peptides;
D O I：
10.1016/j.febslet.2004.04.053
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Ca2+-saturated calmodulin binds to double-length IQ lever-arm sequences from murine myosin-V, forming a 1:1 "bridging" complex with very high affinity, (K-d < 10 pM for double motifs, IQ34, IQ45 and IQ56). Such a 1:1 complex involves interaction of one calmodulin (CaM) molecule with two adjacent IQ-motifs, providing a molecular mechanism for the observed Ca2+-dependent CaM dissociation from the IQ-region. Structural considerations suggest that formation of the 1:1 complex requires a severe distortion of the lever-arm, potentially regulating functional motility. This would be consistent with a recent report of diverse, irregular shapes of the lever arm of myosin-V induced by the presence of Ca2+. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码：166 / 170
页数：5
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