NDLI: Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex

Content Provider	PubMed Central
Author	Brzovic, Peter S. Keeffe, Jennifer R. Nishikawa, Hiroyuki Miyamoto, Keiko Fox, David Fukuda, Mamoru Ohta, Tomohiko Rachel, Klevit
Copyright Year	2003
Abstract	BRCA1 is a breast and ovarian cancer tumor suppressor protein that associates with BARD1 to form a RING/RING heterodimer. The BRCA1/BARD1 RING complex functions as an ubiquitin (Ub) ligase with activity substantially greater than individual BRCA1 or BARD1 subunits. By using NMR spectroscopy and site-directed mutagenesis, we have mapped the binding site on the BRCA1/BARD1 heterodimer for the Ub-conjugating enzyme UbcH5c. The results demonstrate that UbcH5c binds only to the BRCA1 RING domain and not the BARD1 RING. The binding interface is formed by the first and second Zn2+-loops and central α-helix of the BRCA1 RING domain, a region disrupted by cancer-predisposing mutations. Unexpectedly, a second Ub-conjugating enzyme, UbcH7, also interacts with the BRCA1/BARD1 complex with similar affinity, although it is not active in Ub-ligase activity assays. Thus, binding alone is not sufficient for BRCA1-dependent Ub-ligase activity.
Related Links	http://dx.doi.org/10.1073/pnas.0836054100
Ending Page	5651
Page Count	6
Starting Page	5646
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	10
Volume Number	100
Language	English
Publisher	The National Academy of Sciences
Publisher Date	2003-05-13
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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