1b22
From Proteopedia
(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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| - | [[Image:1b22.gif|left|200px]]<br /> | + | [[Image:1b22.gif|left|200px]]<br /><applet load="1b22" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1b22" size=" | + | |
caption="1b22" /> | caption="1b22" /> | ||
'''RAD51 (N-TERMINAL DOMAIN)'''<br /> | '''RAD51 (N-TERMINAL DOMAIN)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Human Rad51 protein (HsRad51) is a homolog of Escherichia coli RecA | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1B22 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1B22 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B22 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ito, Y.]] | [[Category: Ito, Y.]] | ||
[[Category: Kurumizaka, H.]] | [[Category: Kurumizaka, H.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Shibata, T.]] | [[Category: Shibata, T.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:50:40 2008'' |
Revision as of 09:50, 21 February 2008
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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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