3tne

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

spinqualitylabelsall models 3tne, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3tne is a 2 chain structure with sequence from Candida parapsilosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: RIT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CARP1_CANPA Publication Abstract from PubMed 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 A 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. The crystal structure of protease Sapp1p from Candida parapsilosis in complex with the HIV protease inhibitor ritonavir.,Dostal J, Brynda J, Hruskova-Heidingsfeldova O, Pachl P, Pichova I, Rezacova P J Enzyme Inhib Med Chem. 2012 Feb;27(1):160-5. Epub 2011 Dec 6. PMID:22146051 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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