Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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 Proteins. 2007 Aug 15;68(3):738-48. PMID:17510964[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Borelli C, Ruge E, Schaller M, Monod M, Korting HC, Huber R, Maskos K. The crystal structure of the secreted aspartic proteinase 3 from Candida albicans and its complex with pepstatin A. Proteins. 2007 Aug 15;68(3):738-48. PMID:17510964 doi:10.1002/prot.21425
