3DOX

X-ray structure of HIV-1 protease in situ product complex

3DOX の概要

• エントリーDOI: 10.2210/pdb3dox/pdb
• 関連するPDBエントリー: 1G6L 1LV1 2NPH
• 分子名称: HIV-1 PROTEASE, A PEPTIDE SUBSTRATE-SQNY, A PEPTIDE SUBSTRATE-PIV, ... (4 entities in total)
• 機能のキーワード: hiv-1 protease; transition state; reaction intermediate; catalysis; inhibitor; x-ray crystallography, aids, aspartyl protease, capsid maturation, capsid protein, cytoplasm, dna integration, dna recombination, dna-directed dna polymerase, endonuclease, host-virus interaction, hydrolase, lipoprotein, magnesium, metal-binding, multifunctional enzyme, myristate, nuclease, nucleotidyltransferase, nucleus, phosphoprotein, protease, ribosomal frameshifting, rna-binding, rna-directed dna polymerase, transferase, viral nucleoprotein, virion, zinc, zinc-finger
• 由来する生物種: Human immunodeficiency virus type 1 (isolate HXB2 group M subtype B) (HIV-1, HIV-1 M:B_HXB2R); 詳細
• 細胞内の位置: Gag-Pol polyprotein: Host cell membrane; Lipid-anchor . Matrix protein p17: Virion membrane; Lipid- anchor . Capsid protein p24: Virion . Nucleocapsid protein p7: Virion . Reverse transcriptase/ribonuclease H: Virion . Integrase: Virion : P04585
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 22740.68

構造登録者

Hosur, M.V.,Ferrer, J.-L.,Das, A.,Prashar, V.,Bihani, S. (登録日: 2008-07-07, 公開日: 2008-09-09, 最終更新日: 2024-05-29)

主引用文献

Bihani, S.,Das, A.,Prashar, V.,Ferrer, J.-L.,Hosur, M.V.
X-ray structure of HIV-1 protease in situ product complex
Proteins, 74:594-602, 2009

PubMed Abstract: HIV-1 protease is an effective target for design of different types of drugs against AIDS. HIV-1 protease is also one of the few enzymes that can cleave substrates containing both proline and nonproline residues at the cleavage site. We report here the first structure of HIV-1 protease complexed with the product peptides SQNY and PIV derived by in situ cleavage of the oligopeptide substrate SQNYPIV, within the crystals. In the structure, refined against 2.0-A resolution synchrotron data, a carboxyl oxygen of SQNY is hydrogen-bonded with the N-terminal nitrogen atom of PIV. At the same time, this proline nitrogen atom does not form any hydrogen bond with catalytic aspartates. These two observations suggest that the protonation of scissile nitrogen, during peptide bond cleavage, is by a gem-hydroxyl of the tetrahedral intermediate rather than by a catalytic aspartic acid.

PubMed: 18704947
DOI: 10.1002/prot.22174

実験手法

X-RAY DIFFRACTION (2 Å)