4b20
From Proteopedia
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<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=4b20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b20 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b20 RCSB], [http://www.ebi.ac.uk/pdbsum/4b20 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=4b20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b20 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b20 RCSB], [http://www.ebi.ac.uk/pdbsum/4b20 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/NFI_THEMA NFI_THEMA]] Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA. Acts in DNA repair. In vitro, can also cleave single-stranded substrates with inosine, double-stranded DNA with apurinic sites, or DNA sites with uracil or a mismatched base. When present in molar excess, two protein molecules can bind to the same DNA substrate and effect cleavage of both strands (in vitro).<ref>PMID:12081482</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 21:03, 24 December 2014
Structural basis of DNA loop recognition by Endonuclease V
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