2ont
From Proteopedia
(New page: 200px<br /> <applet load="2ont" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ont, resolution 2.400Å" /> '''A swapped dimer of...) |
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| - | [[Image:2ont.gif|left|200px]]<br /> | + | [[Image:2ont.gif|left|200px]]<br /><applet load="2ont" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2ont" size=" | + | |
caption="2ont, resolution 2.400Å" /> | caption="2ont, resolution 2.400Å" /> | ||
'''A swapped dimer of the HIV-1 capsid C-terminal domain'''<br /> | '''A swapped dimer of the HIV-1 capsid C-terminal domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Assembly of the HIV and other retroviruses is primarily driven by the | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2ONT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http:// | + | 2ONT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ONT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ivanov, D.]] | [[Category: Ivanov, D.]] | ||
[[Category: Kasanov, J.]] | [[Category: Kasanov, J.]] | ||
| - | [[Category: Tsodikov, O | + | [[Category: Tsodikov, O V.]] |
[[Category: Wagner, G.]] | [[Category: Wagner, G.]] | ||
[[Category: hiv; capsid; gag; domain swap]] | [[Category: hiv; capsid; gag; domain swap]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:20:38 2008'' |
Revision as of 16:20, 21 February 2008
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A swapped dimer of the HIV-1 capsid C-terminal domain
Overview
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.
About this Structure
2ONT is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
Reference
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
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