1b22

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(New page: 200px<br /> <applet load="1b22" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b22" /> '''RAD51 (N-TERMINAL DOMAIN)'''<br /> ==Overv...)
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Revision as of 13:58, 12 November 2007


1b22

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RAD51 (N-TERMINAL DOMAIN)

Contents

Overview

Human Rad51 protein (HsRad51) is a homolog of Escherichia coli RecA, protein, and functions in DNA repair and recombination. In higher, eukaryotes, Rad51 protein is essential for cell viability. The N-terminal, region of HsRad51 is highly conserved among eukaryotic Rad51 proteins but, is absent from RecA, suggesting a Rad51-specific function for this region., Here, we have determined the structure of the N-terminal part of HsRad51, by NMR spectroscopy. The N-terminal region forms a compact domain, consisting of five short helices, which shares structural similarity with, a domain of endonuclease III, a DNA repair enzyme of E. coli. NMR, experiments did not support the involvement of the N-terminal domain in, HsRad51-HsBrca2 interaction or the self-association of HsRad51 as proposed, by previous studies. However, NMR tiration experiments demonstrated a, physical interaction of the domain with DNA, and allowed mapping of the, DNA binding surface. Mutation analysis showed that the DNA binding surface, is essential for double-stranded and single-stranded DNA binding of, HsRad51. Our results suggest the presence of a DNA binding site on the, outside surface of the HsRad51 filament and provide a possible explanation, for the regulation of DNA binding by phosphorylation within the N-terminal, domain.

Disease

Known diseases associated with this structure: Breast cancer, susceptibility to OMIM:[179617]

About this Structure

1B22 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR., Aihara H, Ito Y, Kurumizaka H, Yokoyama S, Shibata T, J Mol Biol. 1999 Jul 9;290(2):495-504. PMID:10390347

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