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==Crystal Structure of Human NEIL1, Free Protein== | |||
<StructureSection load='5itq' size='340' side='right' caption='[[5itq]], [[Resolution|resolution]] 1.48Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5itq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ITQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ITQ FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5itx|5itx]], [[5ity|5ity]], [[5itt|5itt]], [[5itu|5itu]]</td></tr> | |||
[[Category: | <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=5itq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5itq OCA], [http://pdbe.org/5itq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5itq RCSB], [http://www.ebi.ac.uk/pdbsum/5itq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5itq 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: Lu, L]] | |||
[[Category: Song, J]] | |||
[[Category: Stovicek, O]] | |||
[[Category: Yi, C]] | |||
[[Category: Yue, Z]] | |||
[[Category: Zhang, J]] | |||
[[Category: Zhu, C]] | |||
[[Category: Zong, S]] | |||
[[Category: Dna binding protein-dna complex]] | |||
[[Category: Dna glycosylase neil1 fpg nei base excision repair]] |
Revision as of 21:01, 13 July 2016
Crystal Structure of Human NEIL1, Free ProteinCrystal Structure of Human NEIL1, Free Protein
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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