期刊
PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY
卷 117, 期 2-3, 页码 143-148出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.pbiomolbio.2015.02.003
关键词
BRCT; Tandem BRCT domains; BRCA1; Phosphopeptide; DNA damage response; pSXXF motif
资金
- Wellcome Trust [093167/Z/10/Z]
- UCB
- Biotechnology and Biological Sciences Research Council (BBSRC)
- Biotechnology and Biological Sciences Research Council [1103577] Funding Source: researchfish
- Wellcome Trust [093167/Z/10/Z] Funding Source: Wellcome Trust
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.
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