2JYL
Solution Structure of A Double Mutant of The Carboxy-terminal Dimerization Domain of The HIV-1 Capsid Protein
Summary for 2JYL
| Entry DOI | 10.2210/pdb2jyl/pdb |
| Related | 2jyg |
| Descriptor | Capsid protein p24 (CA) (1 entity in total) |
| Functional Keywords | hiv-1, carboxy-terminal, dimerization domain, ctd, 3d-nmr, capsid protein (ca), double mutant, monomer structure, aids, aspartyl protease, capsid maturation, core protein, cytoplasm, dna integration, dna recombination, dna-directed dna polymerase, endonuclease, hydrolase, lipoprotein, magnesium, membrane, metal-binding, multifunctional enzyme, myristate, nuclease, nucleotidyltransferase, nucleus, phosphoprotein, protease, rna-binding, rna-directed dna polymerase, transferase, viral nucleoprotein, virion, zinc, zinc-finger, viral protein |
| Biological source | Human immunodeficiency virus 1 |
| 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 | 11474.04 |
| Authors | Wong, H.C.,Shin, R.,Krishna, N.R. (deposition date: 2007-12-14, release date: 2008-02-12, Last modification date: 2024-05-29) |
| Primary citation | Wong, H.C.,Shin, R.,Krishna, N.R. Solution Structure of a Double Mutant of the Carboxy-Terminal Dimerization Domain of the HIV-1 Capsid Protein. Biochemistry, 47:2289-2297, 2008 Cited by PubMed Abstract: As in other retroviruses, the HIV-1 capsid (CA) protein is composed of two domains, the N-terminal domain (NTD) and the C-terminal domain (CTD), joined by a flexible linker. The dimerization of the CTD is thought to be a critical step in the assembly of the immature and mature viral capsids. The precise nature of the functional form of CTD dimerization interface has been a subject of considerable interest. Previously, the CTD dimer was thought to involve a face-to-face dimerization observed in the early crystallographic studies. Recently, the crystallographic structure for a domain-swapped CTD dimer has been determined. This dimer, with an entirely different interface that includes the major homology region (MHR) has been suggested as the functional form during the Gag assembly. The structure determination of the monomeric wt CTD of HIV-1 has not been possible because of the monomer-dimer equilibrium in solution. We report the NMR structure of the [W184A/M185A]-CTD mutant in its monomeric form. These mutations interfere with dimerization without abrogating the assembly activity of Gag and CA. The NMR structure shows some important differences compared to the CTD structure in the face-to-face dimer. Notably, the helix-2 is much shorter, and the kink seen in the crystal structure of the wt CTD in the face-to-face dimer is absent. These NMR studies suggest that dimerization-induced conformational changes may be present in the two crystal structures of the CTD dimers and also suggest a mechanism that can simultaneously accommodate both of the distinctly different dimer models playing functional roles during the Gag assembly of the immature capsids. PubMed: 18220423DOI: 10.1021/bi7022128 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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