1xna

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|ACTIVITY=
|ACTIVITY=
|GENE= XRCC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= XRCC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xna FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xna OCA], [http://www.ebi.ac.uk/pdbsum/1xna PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xna RCSB]</span>
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[[Category: xrcc1]]
[[Category: xrcc1]]
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Revision as of 21:52, 30 March 2008


PDB ID 1xna

Drag the structure with the mouse to rotate
Gene: XRCC1 (Homo sapiens)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



NMR SOLUTION STRUCTURE OF THE SINGLE-STRAND BREAK REPAIR PROTEIN XRCC1-N-TERMINAL DOMAIN


Overview

XRCC1 functions in the repair of single-strand DNA breaks in mammalian cells and forms a repair complex with beta-Pol, ligase III and PARP. Here we describe the NMR solution structure of the XRCC1 N-terminal domain (XRCC1 NTD). The structural core is a beta-sandwich with beta-strands connected by loops, three helices and two short two-stranded beta-sheets at each connection side. We show, for the first time, that the XRCC1 NTD specifically binds single-strand break DNA (gapped and nicked). We also show that the XRCC1 NTD binds a gapped DNA-beta-Pol complex. The DNA binding and beta-Pol binding surfaces were mapped by NMR and found to be well suited for interaction with single-strand gap DNA containing a 90 degrees bend, and for simultaneously making contacts with the palm-thumb of beta-Pol in a ternary complex. The findings suggest a mechanism for preferential binding of the XRCC1 NTD to flexible single-strand break DNA.

About this Structure

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

Reference

Solution structure of the single-strand break repair protein XRCC1 N-terminal domain., Marintchev A, Mullen MA, Maciejewski MW, Pan B, Gryk MR, Mullen GP, Nat Struct Biol. 1999 Sep;6(9):884-93. PMID:10467102

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