Candida Research Today is a free monthly online journal that collates and summarizes the latest research about Candida, including details on thrush infections, yeast, diet, treatment, symptoms. | ||||||||
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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, Korting HC, Huber R, Maskos K Department of Dermatology and Allergy, Ludwig Maximilian University of Munich, Frauenlobstr. 9-11, 80337 Munich, Germany. claudia.borelli@med.uni-muenchen.de 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. Published 26 July 2007 in Proteins, 68(3): 738-48.
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