3qg5
From Proteopedia
(Difference between revisions)
| Line 9: | Line 9: | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qg5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qg5 RCSB], [http://www.ebi.ac.uk/pdbsum/3qg5 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qg5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qg5 RCSB], [http://www.ebi.ac.uk/pdbsum/3qg5 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/RAD50_THEMA RAD50_THEMA]] Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50 provides an ATP-dependent control of Mre11 by unwinding and/or repositioning DNA ends into the Mre11 active site (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 22:47, 25 December 2014
The Mre11:Rad50 complex forms an ATP dependent molecular clamp in DNA double-strand break repair
| |||||||||||
