Three-dimensional structure of the Ras-interacting domain of RalGDS

被引：73

作者：

Huang, L

Weng, XW

Hofer, F

Martin, GS

Kim, SH

机构：

[1] UNIV CALIF BERKELEY,LAWRENCE BERKELEY NATL LAB,DEPT CHEM & STRUCT BIOL,DIV EO,BERKELEY,CA 94720

[2] UNIV CALIF BERKELEY,DEPT MOL & CELL BIOL,BERKELEY,CA 94720

来源：

NATURE STRUCTURAL BIOLOGY | 1997年 / 4卷 / 08期

关键词：

D O I：

10.1038/nsb0897-609

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 Ras-interacting domains of the the protein-kinase Raf and the Ral guanine nucleotide dissociation stimulator, RalGDS, lack extensive sequence similarity, but their overall three-dimensional structures are very similar to each other. Mutational analysis indicated that three residues in the RalGDS domain are critical for its interaction with Ras.

引用

页码：609 / 615

页数：7

共 46 条

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