LOCALIZATION AND IDENTIFICATION OF ACTIN STRUCTURES INVOLVED IN THE FILAMIN ACTIN INTERACTION

被引：57

作者：

MEJEAN, C ^{[1
]}

LEBART, MC ^{[1
]}

BOYER, M ^{[1
]}

ROUSTAN, C ^{[1
]}

BENYAMIN, Y ^{[1
]}

机构：

[1] ECOLE PRAT HAUTES ETUD,RECH MOTILITE CELLULAIRE LAB,CNRS,CTR RECH BIOCHIM MACROMOLEC,UPR 8402,F-34033 MONTPELLIER,FRANCE

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1992年 / 209卷 / 02期

关键词：

D O I：

10.1111/j.1432-1033.1992.tb17320.x

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：

The interface between gizzard filamin and skeletal muscle actin was located on the actin monomer. Conserved sequences 105 - 120 and 360 - 372, in the actin subdomain 1 near the myosin binding sites, were involved in this interaction. The corresponding peptides for these sequences were each found to bind filamin and compete in the actin-filamin interaction. When these two peptides were used together in the presence of filamin and filamentous actin, they dissociated sedimentable complexes formed by these two proteins.

引用

页码：555 / 562

页数：8

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