2h6t
From Proteopedia
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Secreted aspartic proteinase (Sap) 3 from Candida albicans complexed with pepstatin A
Overview
The family of secreted aspartic proteinases (Sap) encoded by 10 SAP genes, is an important virulence factor during Candida albicans (C. albicans), infections. Antagonists to Saps could be envisioned to help prevent or, treat candidosis in immunocompromised patients. The knowledge of several, Sap structures is crucial for inhibitor design; only the structure of Sap2, is known. We report the 1.9 and 2.2 A resolution X-ray crystal structures, of Sap3 in a stable complex with pepstatin A and in the absence of an, inhibitor, shedding further light on the enzyme inhibitor binding., Inhibitor binding causes active site closure by the movement of a flap, segment. Comparison of the structures of Sap3 and Sap2 identifies elements, responsible for the specificity of each isoenzyme. Proteins 2007. (c) 2007, Wiley-Liss, Inc.
About this Structure
2H6T is a Single protein structure of sequence from Candida albicans with and as ligands. Active as Candidapepsin, with EC number 3.4.23.24 Full crystallographic information is available from OCA.
Reference
The crystal structure of the secreted aspartic proteinase 3 from Candida albicans and its complex with pepstatin A., Borelli C, Ruge E, Schaller M, Monod M, Christian Korting H, Huber R, Maskos K, Proteins. 2007 May 17;. PMID:17510964
Page seeded by OCA on Wed Jan 23 12:31:35 2008
Categories: Candida albicans | Candidapepsin | Single protein | Borelli, C. | Huber, R. | Maskos, K. | Ruge, E. | IHN | ZN | Aspartic proteinase | Hydrolase
