S-domain assembly of the signal recognition particle

被引：22

作者：

Sauer-Eriksson, AE ^{[1
]}

Hainzl, T ^{[1
]}

机构：

[1] Umea Univ, Umea Ctr Mol Pathogenesis, SE-90187 Umea, Sweden

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2003年 / 13卷 / 01期

关键词：

D O I：

10.1016/S0959-440X(02)00010-6

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 signal recognition particle (SRP) is a phylogenetically conserved ribonucleoprotein that associates with ribosomes to mediate the targeting of membrane and secretory proteins to biological membranes. In higher eukaryotes, SRP biogenesis involves the sequential binding of SRP19 and SRP54 proteins to the S domain of 7S RNA. The recently determined crystal structures of SRP19 in complex with the S domain, and that of the ternary complex of SRP19, the S domain and the M domain of SRP54, provide insight into the molecular basis of S-domain assembly and SRP function.

引用

页码：64 / 70

页数：7

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