5itx: Difference between revisions
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==Crystal Structure of Human NEIL1(P2G R242K) bound to duplex DNA containing Thymine Glycol== | |||
<StructureSection load='5itx' size='340' side='right' caption='[[5itx]], [[Resolution|resolution]] 2.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5itx]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ITX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ITX FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CTG:(5R,6S)-5,6-DIHYDRO-5,6-DIHYDROXYTHYMIDINE-5-MONOPHOSPHATE'>CTG</scene></td></tr> | |||
[[Category: | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ity|5ity]], [[5itq|5itq]], [[5itt|5itt]], [[5itr|5itr]], [[5itu|5itu]]</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=5itx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5itx OCA], [http://pdbe.org/5itx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5itx RCSB], [http://www.ebi.ac.uk/pdbsum/5itx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5itx ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/NEIL1_HUMAN NEIL1_HUMAN]] Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, formamidopyrimidine (Fapy) and 5-hydroxyuracil. Has marginal activity towards 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Has DNA glycosylase/lyase activity towards mismatched uracil and thymine, in particular in U:C and T:C mismatches.<ref>PMID:12200441</ref> <ref>PMID:12509226</ref> <ref>PMID:11904416</ref> <ref>PMID:14522990</ref> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gao, Y]] | |||
[[Category: Liu, M]] | [[Category: Liu, M]] | ||
[[Category: | [[Category: Lu, L]] | ||
[[Category: | [[Category: Song, J]] | ||
[[Category: Stovicek, O]] | [[Category: Stovicek, O]] | ||
[[Category: Yi, C]] | [[Category: Yi, C]] | ||
[[Category: Yue, Z]] | [[Category: Yue, Z]] | ||
[[Category: Zhang, J]] | |||
[[Category: Zhu, C]] | |||
[[Category: Zong, S]] | [[Category: Zong, S]] | ||
[[Category: Dna binding protein-dna complex]] | |||
[[Category: Dna glycosylase neil1 fpg nei base excision repair]] |
Revision as of 21:02, 13 July 2016
Crystal Structure of Human NEIL1(P2G R242K) bound to duplex DNA containing Thymine GlycolCrystal Structure of Human NEIL1(P2G R242K) bound to duplex DNA containing Thymine Glycol
Structural highlights
Function[NEIL1_HUMAN] Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, formamidopyrimidine (Fapy) and 5-hydroxyuracil. Has marginal activity towards 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Has DNA glycosylase/lyase activity towards mismatched uracil and thymine, in particular in U:C and T:C mismatches.[1] [2] [3] [4] References
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