6p40
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of Full Length APOBEC3G FKL== | |
| + | <StructureSection load='6p40' size='340' side='right'caption='[[6p40]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6p40]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P40 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6P40 FirstGlance]. <br> | ||
| + | </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> | ||
| + | <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=6p40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p40 OCA], [http://pdbe.org/6p40 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6p40 RCSB], [http://www.ebi.ac.uk/pdbsum/6p40 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6p40 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | APOBEC3G, a member of the double-domain cytidine deaminase (CD) APOBEC, binds RNA to package into virions and restrict HIV-1 through deamination-dependent or deamination-independent inhibition. Mainly due to lack of a full-length double-domain APOBEC structure, it is unknown how CD1/CD2 domains connect and how dimerization/multimerization is linked to RNA binding and virion packaging for HIV-1 restriction. We report rhesus macaque A3G structures that show different inter-domain packing through a short linker and refolding of CD2. The A3G dimer structure has a hydrophobic dimer-interface matching with that of the previously reported CD1 structure. A3G dimerization generates a surface with intensified positive electrostatic potentials (PEP) for RNA binding and dimer stabilization. Unexpectedly, mutating the PEP surface and the hydrophobic interface of A3G does not abolish virion packaging and HIV-1 restriction. The data support a model in which only one RNA-binding mode is critical for virion packaging and restriction of HIV-1 by A3G. | ||
| - | + | Understanding the structural basis of HIV-1 restriction by the full length double-domain APOBEC3G.,Yang H, Ito F, Wolfe AD, Li S, Mohammadzadeh N, Love RP, Yan M, Zirkle B, Gaba A, Chelico L, Chen XS Nat Commun. 2020 Jan 31;11(1):632. doi: 10.1038/s41467-020-14377-y. PMID:32005813<ref>PMID:32005813</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6p40" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chen, X J]] | ||
| + | [[Category: Li, S X]] | ||
| + | [[Category: Yang, H J]] | ||
| + | [[Category: Apobec3g]] | ||
| + | [[Category: Cytidine deaminase]] | ||
| + | [[Category: Hiv]] | ||
| + | [[Category: Rna binding protein]] | ||
Revision as of 04:18, 13 February 2020
Crystal Structure of Full Length APOBEC3G FKL
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