2JO0

The solution structure of the monomeric species of the C terminal domain of the CA protein of HIV-1

2JO0 の概要

• エントリーDOI: 10.2210/pdb2jo0/pdb
• 関連するPDBエントリー: 1A43
• NMR情報: BMRB: 15137
• 分子名称: Gag-Pol polyprotein (1 entity in total)
• 機能のキーワード: hiv, monomer, capsid protein, viral protein
• 由来する生物種: Human immunodeficiency virus 1
• 細胞内の位置: 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
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9561.01

構造登録者

Alcaraz, L.A.,del Alamo, M.,Barrera, F.N.,Mateu, M.G.,Neira, J.L. (登録日: 2007-02-17, 公開日: 2007-07-31, 最終更新日: 2023-12-20)

主引用文献

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

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: 17526561
DOI: 10.1529/biophysj.106.101089

実験手法

SOLUTION NMR