2ont
From Proteopedia
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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
Page seeded by OCA on Thu Nov 8 14:55:22 2007
