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4pha
From Proteopedia
(Difference between revisions)
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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=4pha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pha OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pha RCSB], [http://www.ebi.ac.uk/pdbsum/4pha 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=4pha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pha OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pha RCSB], [http://www.ebi.ac.uk/pdbsum/4pha PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/DPOLB_HUMAN DPOLB_HUMAN]] Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases.<ref>PMID:9207062</ref> <ref>PMID:9572863</ref> <ref>PMID:11805079</ref> <ref>PMID:21362556</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Koag, M C | + | [[Category: Koag, M C]] |
| - | [[Category: Lee, S | + | [[Category: Lee, S]] |
[[Category: Human dna polymerase beta]] | [[Category: Human dna polymerase beta]] | ||
Revision as of 00:25, 25 December 2014
Structure of human DNA polymerase beta complexed with A in the template base paired with incoming non-hydrolyzable CTP
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