2ont

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[[Image:2ont.gif|left|200px]]
[[Image:2ont.gif|left|200px]]
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{{Structure
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|PDB= 2ont |SIZE=350|CAPTION= <scene name='initialview01'>2ont</scene>, resolution 2.400&Aring;
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|GENE= gag-pol ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 Human immunodeficiency virus 1])
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{{STRUCTURE_2ont| PDB=2ont | SCENE= }}
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|RESOURCES=<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.ebi.ac.uk/pdbsum/2ont PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ont RCSB]</span>
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'''A swapped dimer of the HIV-1 capsid C-terminal domain'''
'''A swapped dimer of the HIV-1 capsid C-terminal domain'''
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[[Category: Tsodikov, O V.]]
[[Category: Tsodikov, O V.]]
[[Category: Wagner, G.]]
[[Category: Wagner, G.]]
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[[Category: capsid]]
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[[Category: Capsid]]
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[[Category: domain swap]]
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[[Category: Domain swap]]
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[[Category: gag]]
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[[Category: Gag]]
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[[Category: hiv]]
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[[Category: Hiv]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:17:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:20:30 2008''
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Revision as of 08:17, 4 May 2008

Template:STRUCTURE 2ont

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 Page seeded by OCA on Sun May 4 11:17:11 2008

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