2ONT
A swapped dimer of the HIV-1 capsid C-terminal domain
Summary for 2ONT
| Entry DOI | 10.2210/pdb2ont/pdb |
| Descriptor | Capsid protein p24 (2 entities in total) |
| Functional Keywords | hiv; capsid; gag; domain swap, viral protein |
| Biological source | Human immunodeficiency virus type 1 (NEW YORK-5 ISOLATE) |
| Cellular location | Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P12497 |
| Total number of polymer chains | 1 |
| Total formula weight | 8540.74 |
| Authors | Ivanov, D.,Tsodikov, O.V.,Kasanov, J.,Ellenberger, T.,Wagner, G.,Collins, T. (deposition date: 2007-01-24, release date: 2007-02-20, Last modification date: 2023-08-30) |
| Primary citation | Ivanov, D.,Tsodikov, O.V.,Kasanov, J.,Ellenberger, T.,Wagner, G.,Collins, T. Domain-swapped dimerization of the HIV-1 capsid C-terminal domain Proc.Natl.Acad.Sci.Usa, 104:4353-4358, 2007 Cited by PubMed Abstract: 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. PubMed: 17360528DOI: 10.1073/pnas.0609477104 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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