View source for 2mzz


==NMR structure of APOBEC3G NTD variant, sNTD==
<StructureSection load='2mzz' size='340' side='right'caption='[[2mzz]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mzz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MZZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MZZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mzz OCA], [https://pdbe.org/2mzz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mzz RCSB], [https://www.ebi.ac.uk/pdbsum/2mzz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mzz ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The human APOBEC3G (A3G) DNA cytosine deaminase restricts and hypermutates DNA-based parasites including HIV-1. The viral infectivity factor (Vif) prevents restriction by triggering A3G degradation. Although the structure of the A3G catalytic domain is known, the structure of the N-terminal Vif-binding domain has proven more elusive. Here, we used evolution- and structure-guided mutagenesis to solubilize the Vif-binding domain of A3G, thus permitting structural determination by NMR spectroscopy. A smaller zinc-coordinating pocket and altered helical packing distinguish the structure from previous catalytic-domain structures and help to explain the reported inactivity of this domain. This soluble A3G N-terminal domain is bound by Vif; this enabled mutagenesis and biochemical experiments, which identified a unique Vif-interacting surface formed by the alpha1-beta1, beta2-alpha2 and beta4-alpha4 loops. This structure sheds new light on the Vif-A3G interaction and provides critical information for future drug development.

Structure of the Vif-binding domain of the antiviral enzyme APOBEC3G.,Kouno T, Luengas EM, Shigematsu M, Shandilya SM, Zhang J, Chen L, Hara M, Schiffer CA, Harris RS, Matsuo H Nat Struct Mol Biol. 2015 May 18. doi: 10.1038/nsmb.3033. PMID:25984970<ref>PMID:25984970</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mzz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Chen L]]
[[Category: Hara M]]
[[Category: Harris RS]]
[[Category: Kouno T]]
[[Category: Luengas EM]]
[[Category: Matsuo H]]
[[Category: Schiffer CA]]
[[Category: Shandilya SMD]]
[[Category: Shigematu M]]
[[Category: Zhang J]]