2JO0
The solution structure of the monomeric species of the C terminal domain of the CA protein of HIV-1
Summary for 2JO0
| Entry DOI | 10.2210/pdb2jo0/pdb |
| Related | 1A43 |
| NMR Information | BMRB: 15137 |
| Descriptor | Gag-Pol polyprotein (1 entity in total) |
| Functional Keywords | hiv, monomer, capsid protein, 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): P35963 |
| Total number of polymer chains | 1 |
| Total formula weight | 9561.01 |
| Authors | Alcaraz, L.A.,del Alamo, M.,Barrera, F.N.,Mateu, M.G.,Neira, J.L. (deposition date: 2007-02-17, release date: 2007-07-31, Last modification date: 2023-12-20) |
| Primary citation | Alcaraz, L.A.,del Alamo, M.,Barrera, F.N.,Mateu, M.G.,Neira, J.L. Flexibility in HIV-1 Assembly Subunits: Solution Structure of the Monomeric C-Terminal Domain of the Capsid Protein Biophys.J., 93:1264-1276, 2007 Cited by PubMed Abstract: The protein CA forms the mature capsid of human immunodeficiency virus. Hexamerization of the N-terminal domain and dimerization of the C-terminal domain, CAC, occur during capsid assembly, and both domains constitute potential targets for anti-HIV inhibitors. CAC homodimerization occurs mainly through its second helix, and is abolished when its sole tryptophan is mutated to alanine. Previous thermodynamic data obtained with the dimeric and monomeric forms of CAC indicate that the structure of the mutant resembles that of a monomeric intermediate found in the folding and association reactions of CAC. We have solved the three-dimensional structure in aqueous solution of the monomeric mutant. The structure is similar to that of the subunits in the dimeric, nonmutated CAC, except the segment corresponding to the second helix, which is highly dynamic. At the end of this region, the polypeptide chain is bent to bury several hydrophobic residues and, as a consequence, the last two helices are rotated 90 degrees when compared to their position in dimeric CAC. The previously obtained thermodynamic data are consistent with the determined structure of the monomeric mutant. This extraordinary ability of CAC to change its structure may contribute to the different modes of association of CA during HIV assembly, and should be taken into account in the design of new drugs against this virus. PubMed: 17526561DOI: 10.1529/biophysj.106.101089 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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