MOTIFS INVOLVED IN PROTEIN-PROTEIN INTERACTIONS

被引：10

作者：

SLINGSBY, C

BATEMAN, OA

SIMPSON, A

机构：

[1] Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, London, WCIE 7HX, Malet Street

来源：

MOLECULAR BIOLOGY REPORTS | 1993年 / 17卷 / 03期

关键词：

MOTIF; DOMAIN; INTERFACE; OLIGOMER; HELIX-BUNDLE; BETA-SHEET;

D O I：

10.1007/BF00986727

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：

Interactions between proteins are extremely variable. However, in the dimeric proteins comprised of regular motifs, interface interactions are similar to those that stabilize monomers. Additional stability is gained by converting loops within motifs or domains to linkers across interfaces. In multi-domain proteins, interactions can be greatly effected by the conformation of linkers between domains. Complex association of subunits, involving higher rotational symmetry or cubic symmetry, frequently involves motif sharing across interfaces. © 1993 Kluwer Academic Publishers.

引用

页码：185 / 195

页数：11

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