2h6t
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The family of secreted aspartic proteinases (Sap) encoded by 10 SAP genes | + | 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. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==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, | + | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17510964 17510964] |
[[Category: Candida albicans]] | [[Category: Candida albicans]] | ||
[[Category: Candidapepsin]] | [[Category: Candidapepsin]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:38:46 2008'' |
Revision as of 15:38, 21 February 2008
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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.
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, Korting HC, Huber R, Maskos K, Proteins. 2007 Aug 15;68(3):738-48. PMID:17510964
Page seeded by OCA on Thu Feb 21 17:38:46 2008
Categories: Candida albicans | Candidapepsin | Single protein | Borelli, C. | Huber, R. | Maskos, K. | Ruge, E. | IHN | ZN | Aspartic proteinase | Hydrolase
