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Structure of N-terminal domain of Candida albicans Als9-2 in complex with human fibrinogen gamma peptideStructure of N-terminal domain of Candida albicans Als9-2 in complex with human fibrinogen gamma peptide
Structural highlights
Publication Abstract from PubMedCandida albicans is the most prevalent fungal pathogen in humans and a major source of life-threatening nosocomial infections. The Als (agglutinin-like sequence) glycoproteins are an important virulence factor for this fungus and have been associated with binding of host-cell surface proteins and small peptides of random sequence, the formation of biofilms and amyloid fibers. High-resolution structures of N-terminal Als adhesins (NT-Als; up to 314 amino acids) show that ligand recognition relies on a motif capable of binding flexible C termini of peptides in extended conformation. Central to this mechanism is an invariant lysine that recognizes the C-terminal carboxylate of ligands at the end of a deep-binding cavity. In addition to several protein-peptide interactions, a network of water molecules runs parallel to one side of the ligand and contributes to the recognition of diverse peptide sequences. These data establish NT-Als adhesins as a separate family of peptide-binding proteins and an unexpected adhesion system for primary, widespread protein-protein interactions at the Candida/host-cell interface. Structural basis for the broad specificity to host-cell ligands by the pathogenic fungus Candida albicans.,Salgado PS, Yan R, Taylor JD, Burchell L, Jones R, Hoyer LL, Matthews SJ, Simpson PJ, Cota E Proc Natl Acad Sci U S A. 2011 Sep 20;108(38):15775-9. Epub 2011 Sep 6. PMID:21896717[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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