Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif

被引：27

作者：

Wu, Qian ^{[1
]}

Jubb, Harry ^{[1
]}

Blundell, Tom L. ^{[1
]}

机构：

[1] Univ Cambridge, Dept Biochem, Cambridge CB2 1GA, England

来源：

PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY | 2015年 / 117卷 / 2-3期

基金：

英国惠康基金; 英国生物技术与生命科学研究理事会;

关键词：

BRCT; Tandem BRCT domains; BRCA1; Phosphopeptide; DNA damage response; pSXXF motif; CANCER SUSCEPTIBILITY GENE; TUMOR-SUPPRESSOR BRCA1; BREAST-CANCER; STRUCTURAL BASIS; OVARIAN-CANCER; PHOSPHOPROTEIN BINDING; CRYSTAL-STRUCTURE; PROTEIN; MUTATIONS; REPEATS;

D O I：

10.1016/j.pbiomolbio.2015.02.003

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：

BRCA1 BRCT domains function as phosphoprotein-binding modules for recognition of the phosphorylated protein-sequence motif pSXXF. While the motif interaction interface provides strong anchor points for binding, protein regions outside the motif have recently been found to be important for binding affinity. In this review, we compare the available structural data for BRCA1 BRCT domains in complex with phosphopeptides in order to gain a more complete understanding of the interaction between phosphopeptides and BRCA1-BRCT domains. (C) 2015 The Authors. Published by Elsevier Ltd.

引用

页码：143 / 148

页数：6

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