Abstract
Carboxy terminal BRCT domains of the breast cancer susceptibility gene 1 (BRCA1) bind to phosphorylated proteins through a pSXXF consensus recognition motif. We report a systematic structure-activity relationship study that maps the BRCT(BRCA1)-pSXXF binding interface, leading to identification of peptides with nanomolar binding affinities comparable to those of the previously reported 13-mer peptides and providing a clear description of the pSXXF-BRCT interface, which is essential for developing small molecule inhibitors via the peptidomimetic approach.
Original language | English (US) |
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Pages (from-to) | 4264-4268 |
Number of pages | 5 |
Journal | Journal of Medicinal Chemistry |
Volume | 54 |
Issue number | 12 |
DOIs | |
State | Published - Jun 23 2011 |
ASJC Scopus subject areas
- Molecular Medicine
- Drug Discovery