ArticleProtein science : a publication of the Protein Society1996
Structure of a secreted aspartic protease from C. albicans complexed with a potent inhibitor: implications for the design of antifungal agents.
Article in Protein science : a publication of the Protein Society, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Structural and Functional Insights into Viral and Fungal Proteins Involved in Chronic Inflammation and Their Biologic Treatments.Pharmaceutics · 2025Review
- Secreted Aspartic Proteinases: Key Factors inInternational journal of molecular sciences · 2024Review
- Computational modelling of the antimicrobial peptides Cruzioseptin-4 extracted from the frog Cruziohyla calcarifer and Pictuseptin-1 extracted from the frog Boana picturata.Scientific reports · 2024Article
- Antioxidant, Volatile Compounds; Antimicrobial, Anti-Inflammatory, and Dermatoprotective Properties ofMolecules (Basel, Switzerland) · 2023Article
- Current Status and Perspectives of Protease Inhibitors and Their Combination with Nanosized Drug Delivery Systems for Targeted Cancer Therapy.Drug design, development and therapy · 2021Review
- Aspartic peptidase ofJournal of enzyme inhibition and medicinal chemistry · 2020Article
- Extensive expansion of A1 family aspartic proteinases in fungi revealed by evolutionary analyses of 107 complete eukaryotic proteomes.Genome biology and evolution · 2014Article
- Protease expression by microorganisms and its relevance to crucial physiological/pathological events.World journal of biological chemistry · 2011Article
- HIV aspartyl protease inhibitors as promising compounds against Candida albicans André Luis Souza dos Santos.World journal of biological chemistry · 2010Article
- Evidence that the Bacillus subtilis SpoIIGA protein is a novel type of signal-transducing aspartic protease.The Journal of biological chemistry · 2008Article
- Candida albicans secreted aspartyl proteinases in virulence and pathogenesis.Microbiology and molecular biology reviews : MMBR · 2003Review
- Analysis of crystal structures of aspartic proteinases: on the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes.Protein science : a publication of the Protein Society · 2001Article
- Effects of the human immunodeficiency virus (HIV) proteinase inhibitors saquinavir and indinavir on in vitro activities of secreted aspartyl proteinases of Candida albicans isolates from HIV-infected patients.Antimicrobial agents and chemotherapy · 1999Article
- Cell wall and secreted proteins of Candida albicans: identification, function, and expression.Microbiology and molecular biology reviews : MMBR · 1998Review
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8 authors.
Funding
Abstract
The three-dimensional structure of a secreted aspartic protease from Candida albicans complexed with a potent inhibitor reveals variations on the classical aspartic protease theme that dramatically alter the specificity of this class of enzymes. The structure presents: (1) an 8-residue insertion near the first disulfide (Cys 45-Cys 50, pepsin numbering) that results in a broad flap extending toward the active site; (2) a 7-residue deletion replacing helix hN2 (Ser 110-Tyr 114), which enlarges the S3 pocket; (3) a short polar connection between the two rigid body domains that alters their relative orientation and provides certain specificity; and (4) an ordered 11-residue addition at the carboxy terminus. The inhibitor binds in an extended conformation and presents a branched structure at the P3 position. The implications of these findings for the design of potent antifungal agents are discussed.
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