4row

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'''Unreleased structure'''
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==The crystal structure of novel APOBEC3G CD2 head-to-tail dimer suggests the binding mode of full-length APOBEC3G to HIV-1 ssDNA==
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<StructureSection load='4row' size='340' side='right' caption='[[4row]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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The entry 4row is ON HOLD
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4row]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ROW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ROW FirstGlance]. <br>
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Authors: Lu, X., Zhang, T., Xu, Z., Liu, S., Zhao, B., Lan, W., Wang, C., Ding, J., Cao, C.
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jyw|2jyw]], [[4rov|4rov]]</td></tr>
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Description: The crystal structure of novel APOBEC3G CD2 head-to-tail dimer suggests the binding mode of full-length APOBEC3G to HIV-1 ssDNA
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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=4row FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4row OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4row RCSB], [http://www.ebi.ac.uk/pdbsum/4row PDBsum]</span></td></tr>
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[[Category: Unreleased Structures]]
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</table>
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[[Category: Ding, J]]
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== Function ==
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[[Category: Zhang, T]]
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[[http://www.uniprot.org/uniprot/ABC3G_HUMAN ABC3G_HUMAN]] DNA deaminase (cytidine deaminase) that mediates a form of innate resistance to retroviral infections (at least to HIV-1 infection) by triggering G-to-A hypermutation in the newly synthesized viral DNA. The replacements C-to-U in the minus strand DNA of HIV-1 during reverse transcription, leads to G-to-A transitions in the plus strand. The inhibition of viral replication is either due to the degradation of the minus strand before its integration or to the lethality of the hypermutations. Modification of both DNA strands is not excluded. This antiviral activity is neutralized by the virion infectivity factor (VIF), that prevents the incorporation of APOBEC3G into progeny HIV-1 virions by both inhibiting its translation and/or by inducing its ubiquitination and subsequent degradation by the 26S proteasome. May also prevent the transposition of a subset of retroelements. Binds a variety of RNAs, but does not display detectable APOB, NF1 and NAT1 mRNA editing.<ref>PMID:14557625</ref> <ref>PMID:12167863</ref> <ref>PMID:12808466</ref> <ref>PMID:12809610</ref> <ref>PMID:12808465</ref> <ref>PMID:12859895</ref> <ref>PMID:12970355</ref> <ref>PMID:14528300</ref> <ref>PMID:15031497</ref> <ref>PMID:16527742</ref> <ref>PMID:21123384</ref> <ref>PMID:18288108</ref>
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[[Category: Lu, X]]
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== References ==
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[[Category: Zhao, B]]
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<references/>
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[[Category: Liu, S]]
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__TOC__
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</StructureSection>
[[Category: Cao, C]]
[[Category: Cao, C]]
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[[Category: Ding, J]]
[[Category: Lan, W]]
[[Category: Lan, W]]
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[[Category: Liu, S]]
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[[Category: Lu, X]]
[[Category: Wang, C]]
[[Category: Wang, C]]
[[Category: Xu, Z]]
[[Category: Xu, Z]]
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[[Category: Zhang, T]]
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[[Category: Zhao, B]]
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[[Category: Deamination]]
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[[Category: Dna binding]]
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[[Category: Dna deamination]]
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[[Category: Hydrolase]]
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[[Category: Zinc finger]]

Revision as of 14:53, 31 December 2014

The crystal structure of novel APOBEC3G CD2 head-to-tail dimer suggests the binding mode of full-length APOBEC3G to HIV-1 ssDNA

4row, resolution 1.70Å

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OCA

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