1b22: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1b22.gif|left|200px]]
{{Seed}}
[[Image:1b22.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1b22|  PDB=1b22  |  SCENE=  }}  
{{STRUCTURE_1b22|  PDB=1b22  |  SCENE=  }}  


'''RAD51 (N-TERMINAL DOMAIN)'''
===RAD51 (N-TERMINAL DOMAIN)===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_10390347}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10390347 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_10390347}}


==About this Structure==
==About this Structure==
1B22 is a [[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].  
1B22 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B22 OCA].  


==Reference==
==Reference==
Line 32: Line 36:
[[Category: Rsgi]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:57:57 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:03:36 2008''

Revision as of 15:03, 30 June 2008

File:1b22.png

Template:STRUCTURE 1b22

RAD51 (N-TERMINAL DOMAIN)

Template:ABSTRACT PUBMED 10390347

About this Structure

1B22 is a Single protein structure of sequence from Homo sapiens. Full experimental 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

Page seeded by OCA on Mon Jun 30 18:03:36 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA