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| {{STRUCTURE_2ont| PDB=2ont | SCENE= }} | | {{STRUCTURE_2ont| PDB=2ont | SCENE= }} |
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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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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17360528}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17360528 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17360528}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Gag]] | | [[Category: Gag]] |
| [[Category: Hiv]] | | [[Category: Hiv]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:17:11 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:26:42 2008'' |