Structure-activity relationship studies to probe the phosphoprotein binding site on the carboxy terminal domains of the breast cancer susceptibility gene 1

Ziyan Yuan, Eric A. Kumar, Smitha Kizhake, Amarnath Natarajan

Research output: Contribution to journalArticle

14 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)4264-4268
Number of pages5
JournalJournal of Medicinal Chemistry
Volume54
Issue number12
DOIs
StatePublished - Jun 23 2011

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Neoplasm Genes
Phosphoproteins
Structure-Activity Relationship
Binding Sites
Breast Neoplasms
Peptidomimetics
Peptides
Proteins

ASJC Scopus subject areas

  • Molecular Medicine
  • Drug Discovery

Cite this

Structure-activity relationship studies to probe the phosphoprotein binding site on the carboxy terminal domains of the breast cancer susceptibility gene 1. / Yuan, Ziyan; Kumar, Eric A.; Kizhake, Smitha; Natarajan, Amarnath.

In: Journal of Medicinal Chemistry, Vol. 54, No. 12, 23.06.2011, p. 4264-4268.

Research output: Contribution to journalArticle

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