4ph0
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==capsid protein from bovine leukemia virus== | |
| + | <StructureSection load='4ph0' size='340' side='right'caption='[[4ph0]], [[Resolution|resolution]] 2.75Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4ph0]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovine_leukemia_virus Bovine leukemia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PH0 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7497Å</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=4ph0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ph0 OCA], [https://pdbe.org/4ph0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ph0 RCSB], [https://www.ebi.ac.uk/pdbsum/4ph0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ph0 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A7KWZ1_BLV A7KWZ1_BLV] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Retroviruses depend upon self-assembly of their capsid proteins (core particle) to yield infectious mature virions. Despite the essential role of the retroviral core, its high polymorphism has hindered high-resolution structural analyses. Here, we report the x-ray structure of the native capsid (CA) protein from bovine leukemia virus. CA is organized as hexamers that deviate significantly from 6-fold symmetry, yet adjust to make two-dimensional pseudo-hexagonal arrays that mimic mature retroviral cores. Intra- and interhexameric quasi-equivalent contacts are uncovered, with flexible trimeric lateral contacts among hexamers, yet preserving very similar dimeric interfaces making the lattice. The conformation of each capsid subunit in the hexamer is therefore dictated by long-range interactions, revealing how the hexamers can also assemble into closed core particles, a relevant feature of retrovirus biology. | ||
| - | + | Conformational plasticity of a native retroviral capsid revealed by x-ray crystallography.,Obal G, Trajtenberg F, Carrion F, Tome L, Larrieux N, Zhang X, Pritsch O, Buschiazzo A Science. 2015 Jun 4. pii: aaa5182. PMID:26044299<ref>PMID:26044299</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 4ph0" style="background-color:#fffaf0;"></div> |
| - | [[Category: Buschiazzo | + | == References == |
| - | [[Category: Obal | + | <references/> |
| - | [[Category: Trajtenberg | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Bovine leukemia virus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Buschiazzo A]] | ||
| + | [[Category: Obal G]] | ||
| + | [[Category: Pritsch O]] | ||
| + | [[Category: Trajtenberg F]] | ||
Current revision
capsid protein from bovine leukemia virus
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