7agb | pdb_00007agb

Protease Sapp1p from Candida parapsilosis in complex with KB70

spinqualitylabelsall models 7agb, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7agb is a 8 chain structure with sequence from Candida parapsilosis and Streptomyces albus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: 1PE, BOC, MES, NA, PE3, PGE, PSA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CARP1_CANPA Publication Abstract from PubMed Pathogenic Candida albicans yeasts frequently cause infections in hospitals. Antifungal drugs lose effectiveness due to other Candida species and resistance. New medications are thus required. Secreted aspartic protease of C. parapsilosis (Sapp1p) is a promising target. We have thus solved the crystal structures of Sapp1p complexed to four peptidomimetic inhibitors. Three potent inhibitors (K(i): 0.1, 0.4, 6.6 nM) resembled pepstatin A (K(i): 0.3 nM), a general aspartic protease inhibitor, in terms of their interactions with Sapp1p. However, the weaker inhibitor (K(i): 14.6 nM) formed fewer nonpolar contacts with Sapp1p, similarly to the smaller HIV protease inhibitor ritonavir (K(i): 1.9 microM), which, moreover, formed fewer H-bonds. The analyses have revealed the structural determinants of the subnanomolar inhibition of C. parapsilosis aspartic protease. Because of the high similarity between Saps from different Candida species, these results can further be used for the design of potent and specific Sap inhibitor-based antimycotic drugs. Structural determinants for subnanomolar inhibition of the secreted aspartic protease Sapp1p from Candida parapsilosis.,Dostal J, Brynda J, Vankova L, Zia SR, Pichova I, Heidingsfeld O, Lepsik M J Enzyme Inhib Med Chem. 2021 Dec;36(1):914-921. doi: , 10.1080/14756366.2021.1906664. PMID:33843395 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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