5cqh
From Proteopedia
(Difference between revisions)
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- | ''' | + | ==Crystal Structure of the Cancer Genomic DNA Mutator APOBEC3B== |
- | + | <StructureSection load='5cqh' size='340' side='right' caption='[[5cqh]], [[Resolution|resolution]] 1.73Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[5cqh]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CQH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CQH FirstGlance]. <br> | |
- | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
- | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cqd|5cqd]], [[5cqi|5cqi]], [[5cqk|5cqk]]</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=5cqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cqh OCA], [http://pdbe.org/5cqh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cqh RCSB], [http://www.ebi.ac.uk/pdbsum/5cqh PDBsum]</span></td></tr> | |
- | [[ | + | </table> |
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/ABC3B_HUMAN ABC3B_HUMAN]] DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single-or double-stranded RNA. Exhibits antiviral activity against simian immunodeficiency virus (SIV), hepatitis B virus (HBV) and human T-cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility of LTR and non-LTR retrotransposons.<ref>PMID:12859895</ref> <ref>PMID:15466872</ref> <ref>PMID:16060832</ref> <ref>PMID:16527742</ref> <ref>PMID:20062055</ref> <ref>PMID:22457529</ref> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Aihara, H]] | [[Category: Aihara, H]] | ||
- | [[Category: Shi, K]] | ||
[[Category: Kurahashi, K]] | [[Category: Kurahashi, K]] | ||
+ | [[Category: Shi, K]] | ||
+ | [[Category: Apobec]] | ||
+ | [[Category: Deaminase]] | ||
+ | [[Category: Hydrolase]] |
Revision as of 13:52, 7 October 2015
Crystal Structure of the Cancer Genomic DNA Mutator APOBEC3B
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Categories: Aihara, H | Kurahashi, K | Shi, K | Apobec | Deaminase | Hydrolase