Phosphoserine/threonine binding domains: You can't pSERious?

被引：70

作者：

Yaffe, MB

Smerdon, SJ

机构：

[1] MIT, Ctr Canc Res, Cambridge, MA 02139 USA

[2] Natl Inst Med Res, Div Prot Struct, London NW7 1AA, England

来源：

STRUCTURE | 2001年 / 9卷 / 03期

关键词：

D O I：

10.1016/S0969-2126(01)00580-9

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 fundamental biological importance of protein phosphorylation is underlined by the existence of more than 500 protein kinase genes within the human genome. In many cases, phosphorylation on serine, threonine, and tyrosine residues creates binding surfaces for a variety of phospho-amino acid binding proteins/modules. Here, we review the insights into serine/threonine phosphorylation-dependent signal transduction processes provided by structures of several of these proteins and their complexes.

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页码：R33 / R38

页数：6

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