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) |
|---|---|
| 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
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Yuan, Z., Kumar, E. A., Kizhake, S., & Natarajan, A. (2011). Structure-activity relationship studies to probe the phosphoprotein binding site on the carboxy terminal domains of the breast cancer susceptibility gene 1. Journal of Medicinal Chemistry, 54(12), 4264-4268. https://doi.org/10.1021/jm1016413