2ont: Difference between revisions
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==A swapped dimer of the HIV-1 capsid C-terminal domain== | |||
<StructureSection load='2ont' size='340' side='right' caption='[[2ont]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2ont]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_(new_york-5_isolate) Human immunodeficiency virus type 1 (new york-5 isolate)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ONT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ONT FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gag-pol ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11698 Human immunodeficiency virus type 1 (NEW YORK-5 ISOLATE)])</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=2ont FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ont OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ont RCSB], [http://www.ebi.ac.uk/pdbsum/2ont PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Assembly of the HIV and other retroviruses is primarily driven by the oligomerization of the Gag polyprotein, the major viral structural protein capable of forming virus-like particles even in the absence of all other virally encoded components. Several critical determinants of Gag oligomerization are located in the C-terminal domain of the capsid protein (CA-CTD), which encompasses the most conserved segment in the highly variable Gag protein called the major homology region (MHR). The CA-CTD is thought to function as a dimerization module, although the existing model of CA-CTD dimerization does not readily explain why the conserved residues of the MHR are essential for retroviral assembly. Here we describe an x-ray structure of a distinct domain-swapped variant of the HIV-1 CA-CTD dimer stabilized by a single amino acid deletion. In the domain-swapped structure, the MHR-containing segment forms a major part of the dimerization interface, providing a structural mechanism for the enigmatic function of the MHR in HIV assembly. Our observations suggest that swapping of the MHR segments of adjacent Gag molecules may be a critical intermediate in retroviral assembly. | |||
Domain-swapped dimerization of the HIV-1 capsid C-terminal domain.,Ivanov D, Tsodikov OV, Kasanov J, Ellenberger T, Wagner G, Collins T Proc Natl Acad Sci U S A. 2007 Mar 13;104(11):4353-8. Epub 2007 Mar 5. PMID:17360528<ref>PMID:17360528</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Virus coat protein|Virus coat protein]] | *[[Virus coat protein|Virus coat protein]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: Collins, T | </StructureSection> | ||
[[Category: Ellenberger, T | [[Category: Collins, T]] | ||
[[Category: Ivanov, D | [[Category: Ellenberger, T]] | ||
[[Category: Kasanov, J | [[Category: Ivanov, D]] | ||
[[Category: Tsodikov, O V | [[Category: Kasanov, J]] | ||
[[Category: Wagner, G | [[Category: Tsodikov, O V]] | ||
[[Category: Wagner, G]] | |||
[[Category: Capsid]] | [[Category: Capsid]] | ||
[[Category: Domain swap]] | [[Category: Domain swap]] | ||
Revision as of 13:48, 17 December 2014
A swapped dimer of the HIV-1 capsid C-terminal domain
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