DEFINITION OF AN INTERFACE IMPLICATED IN GELSOLIN BINDING TO THE SIDES OF ACTIN-FILAMENTS

被引：13

作者：

FEINBERG, J

BENYAMIN, Y

ROUSTAN, C

机构：

[1] UNIV MONTPELLIER 1,CTR RECH BIOCHIM MACROMOLEC,CNRS,UPR 9008,INSERM,U249,F-34033 MONTPELLIER,FRANCE

[2] EPHE,RECH MOTIL CELLULAIRE LAB,F-34033 MONTPELLIER,FRANCE

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1995年 / 209卷 / 02期

关键词：

D O I：

10.1006/bbrc.1995.1520

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：

Whereas the interaction of the N-terminal domain of gelsolin with monomeric actin is well known, the location of domains 2-3 interacting with the actin filament during the severing process remains uncertain. In this study we define an interface that supports binding of gelsolin domain 2 along the filament axis. Using specific antibodies and actin peptides, this interface was restricted to two adjacent segments: 1-10 and 18-28 in the N-terminal part of actin sequence. (C) 1995 Academic Press, Inc.

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收藏

页码：426 / 432

页数：7

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