Molecular modeling of the myosin-S1(A1) isoform

被引：38
作者：
Aydt, Ewald M.
Wolff, Gerhard
Morano, Ingo
机构：
[1] Max Delbruck Ctr Mol Med, D-13122 Berlin, Germany
[2] Revotar Biopharmaceut AG, Hennigsdorf, Germany
[3] Univ Med Berlin, Charite, Johannes Muller Inst Physiol, Berlin, Germany
来源：
JOURNAL OF STRUCTURAL BIOLOGY | 2007年 / 159卷 / 01期
关键词：
myosin; molecular modeling; 3D-structure; essential myosin light chain;
D O I：
10.1016/j.jsb.2007.04.002
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：
Type II myosin is the molecular motor which drives contraction upon cyclic interaction with filamentous actin while consuming ATP. The contemporary crystallographic structure of the myosin subfragment-1 (S1) of myosin covers both the motor domain of the heavy chain (MHC) as well as the essential (ELC) and regulatory light chains (RLC). A part of the N-terminus of the ELC is, however, missing in the 3D-models of Type II myosin. The N-terminal domain of the ELC comprises interesting functional features since it binds to actin thus controlling myosin motor activity. For the first time, we modeled the missing 46 N-terminal amino acid of the ELC to the contemporary actin-myosin-S1 complex. We show a rod-like 91 A structure being long enough to bridge the gap between the ELC core of myosin-SI and the appropriate binding site of the ELC on the actin filament. (c) 2007 Elsevier Inc. All rights reserved.
引用
收藏
页码：158 / 163
页数：6
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