View source for 2ont


==A swapped dimer of the HIV-1 capsid C-terminal domain==
<StructureSection load='2ont' size='340' side='right'caption='[[2ont]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ont]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2ONT 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]] 2.4&#8491;</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=2ont FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ont OCA], [https://pdbe.org/2ont PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ont RCSB], [https://www.ebi.ac.uk/pdbsum/2ont PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ont ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9IVQ4_9HIV1 Q9IVQ4_9HIV1] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ont" style="background-color:#fffaf0;"></div>

==See Also==
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Collins T]]
[[Category: Ellenberger T]]
[[Category: Ivanov D]]
[[Category: Kasanov J]]
[[Category: Tsodikov OV]]
[[Category: Wagner G]]