BRCT domains: phosphopeptide binding and signaling modules
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Updated: Jul 4, 2026

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
Published on: August 13, 2012
Maria C Rodriguez1, Zhou Songyang
11Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA.
Abstract:
The BRCA1 C-terminus (BRCT) domains are essential for the tumor suppressor function of BRCA1, and have been found in a variety of proteins from bacteria to men. Recent studies demonstrate that the BRCT domain constitutes a novel phosphopeptide binding region. In this review we seek to discuss the recent biochemical and structural data that have helped elucidate the molecular basis of BRCT domain function and BRCT-mediated interactions, with special emphasis on the role of phospho-specific interactions in key networks that regulate DNA repair. Finally we offer predictions on additional phospho-interacting BRCT domains and potential in vivo binding sites for several BRCT domains.
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