2ont: Difference between revisions
No edit summary |
No edit summary |
||
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= gag-pol ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 Human immunodeficiency virus 1]) | |GENE= gag-pol ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 Human immunodeficiency virus 1]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|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> | |||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Tsodikov, O V.]] | [[Category: Tsodikov, O V.]] | ||
[[Category: Wagner, G.]] | [[Category: Wagner, G.]] | ||
[[Category: | [[Category: capsid]] | ||
[[Category: domain swap]] | |||
[[Category: gag]] | |||
[[Category: hiv]] | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:20:30 2008'' | ||
Revision as of 04:20, 31 March 2008
| |||||||
| , resolution 2.400Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | gag-pol (Human immunodeficiency virus 1) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
A swapped dimer of the HIV-1 capsid C-terminal domain
OverviewOverview
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 StructureAbout this Structure
2ONT is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
ReferenceReference
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 Mon Mar 31 04:20:30 2008