Evidence for an actin binding helix in gelsolin segment 2; Have homologous sequences in segments 1 and 2 of gelsolin evolved to divergent actin binding functions?

被引：19

作者：

VanTroys, M ^{[1
]}

Dewitte, D ^{[1
]}

Goethals, M ^{[1
]}

Vandekerckhove, J ^{[1
]}

Ampe, C ^{[1
]}

机构：

[1] STATE UNIV GHENT VIB, FAC MED, DEPT BIOCHEM, B-9000 GHENT, BELGIUM

来源：

FEBS LETTERS | 1996年 / 397卷 / 2-3期

关键词：

crosslinking; F-actin binding; gelsolin; peptide mimetic;

D O I：

10.1016/S0014-5793(96)01086-1

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：

Gelsolin is built up of six homologous segments that perform different functions on actin, Segments 1 and 2, which are suggested to be highly similar in their overall folds, bind monomeric and filamentous actin respectively, A long alpha-helix in segment 1 forms the major contact site of this segment with actin, We show that sequence 197-226 of segment 2, equivalent to the region around the actin binding helix in segment 1, contains F-actin binding activity, Consequently, positionally similar parts of segment 1 and 2 are implicated in the actin contact and solvent exposed residues in these parts must have evolved differentially to meet their different actin binding properties.

引用

页码：191 / 196

页数：6

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