N-terminal myosin-binding fragment of talin

被引：9

作者：

Lin, Y ^{[1
]}

Kishi, H ^{[1
]}

Nakamura, A ^{[1
]}

Takagi, T ^{[1
]}

Kohama, K ^{[1
]}

机构：

[1] Gunma Univ, Sch Med, Dept Pharmacol, Gunma 3718511, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1998年 / 249卷 / 03期

基金：

日本学术振兴会;

关键词：

talin; N-terminal 47 KDa fragment; myosin binding; ATPase stimulation;

D O I：

10.1006/bbrc.1998.9000

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：

Talin, an actin-binding protein from smooth muscle, is shown to bind to myosin in such a way that it stimulates the ATPase activity of myosin irrespective of the phosphorylation state of myosin. The binding site is shown to be localized at the N-terminal, 47 KDa fragment. The position of the actin-binding site at the C terminal suggests that talin may work as a crosslinker between myosin and actin. (C) 1998 Academic Press.

引用

页码：656 / 659

页数：4

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