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Structural characterization of BRCT-tetrapeptide binding interactions.

Abstract：

:BRCT(BRCA1) plays a major role in DNA repair pathway, and does so by recognizing the conserved sequence pSXXF in its target proteins. Remarkably, tetrapeptides containing pSXXF motif bind with high specificity and micromolar affinity. Here, we have characterized the binding interactions of pSXXF tetrapeptides using NMR spectroscopy and calorimetry. We show that BRCT is dynamic and becomes structured on binding, that pSer and Phe residues dictate overall binding, and that the binding affinities of the tetrapeptides are intimately linked to structural and dynamic changes both in the BRCT(BRCA1) and tetrapeptides. These results provide critical insights for designing high-affinity BRCT(BRCA1) inhibitors.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Joseph PR,Yuan Z,Kumar EA,Lokesh GL,Kizhake S,Rajarathnam K,Natarajan A

doi

10.1016/j.bbrc.2010.01.098

subject

Has Abstract

pub_date

2010-03-05 00:00:00

pages

207-10

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(10)00147-6

journal_volume

393

pub_type

杂志文章

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