3TNE

The crystal structure of protease Sapp1p from Candida parapsilosis in complex with the HIV protease inhibitor ritonavir

3TNE の概要

• エントリーDOI: 10.2210/pdb3tne/pdb
• 関連するPDBエントリー: 3FV3
• 関連するBIRD辞書のPRD_ID: PRD_001001
• 分子名称: Secreted aspartic protease, RITONAVIR (3 entities in total)
• 機能のキーワード: aspartic acid endopeptidases, catalytic domain, ritonavir, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Candida parapsilosis (Yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 73172.21

構造登録者

Dostal, J.,Brynda, J.,Hruskova-Heidingsfeldova, O.,Pachl, P.,Pichova, I.,Rezacova, P. (登録日: 2011-09-01, 公開日: 2012-03-07, 最終更新日: 2024-11-27)

主引用文献

Dostal, J.,Brynda, J.,Hruskova-Heidingsfeldova, O.,Pachl, P.,Pichova, I.,Rezacova, P.
The crystal structure of protease Sapp1p from Candida parapsilosis in complex with the HIV protease inhibitor ritonavir.
J Enzyme Inhib Med Chem, 27:160-165, 2012

PubMed Abstract: Secreted aspartic proteases (Saps) are extracellular proteolytic enzymes that enhance the virulence of Candida pathogens. These enzymes therefore represent possible targets for therapeutic drug design. Saps are inhibited by nanomolar concentrations of the classical inhibitor of aspartic proteases pepstatin A and also by the inhibitors of the HIV protease, but with the K(i) of micromolar values or higher. To contribute to the discussion regarding whether HIV protease inhibitors can act against opportunistic mycoses by the inhibition of Saps, we determined the structure of Sapp1p from Candida parapsilosis in complex with ritonavir (RTV), a clinically used inhibitor of the HIV protease. The crystal structure refined at resolution 2.4 Å proved binding of RTV into the active site of Sapp1p and provided the structural information necessary to evaluate the stability and specificity of the protein-inhibitor interaction.

PubMed: 22146051
DOI: 10.3109/14756366.2011.627508

実験手法

X-RAY DIFFRACTION (2.4 Å)