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 [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]] 2.4Å</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®/PubMed®, 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: | [[Category: Tsodikov OV]] | ||
[[Category: Wagner G]] | |||
[[Category: Collins | |||
[[Category: Ellenberger | |||
[[Category: Ivanov | |||
[[Category: Kasanov | |||
[[Category: Tsodikov | |||
[[Category: Wagner | |||
Latest revision as of 13:45, 30 August 2023
A swapped dimer of the HIV-1 capsid C-terminal domainA swapped dimer of the HIV-1 capsid C-terminal domain
Structural highlights
FunctionPublication Abstract from PubMedAssembly 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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