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2y7m
From Proteopedia
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| - | + | ==Structure of N-terminal domain of Candida albicans als9-2 (Pt derivative)== | |
| - | + | <StructureSection load='2y7m' size='340' side='right'caption='[[2y7m]], [[Resolution|resolution]] 1.98Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2y7m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y7M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y7M FirstGlance]. <br> | |
| - | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2y7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y7m OCA], [https://pdbe.org/2y7m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y7m RCSB], [https://www.ebi.ac.uk/pdbsum/2y7m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y7m ProSAT]</span></td></tr> | |
| - | -- | + | </table> |
| - | + | == Function == | |
| + | [https://www.uniprot.org/uniprot/ALS9_CANAL ALS9_CANAL] Cell surface adhesion protein which mediates both yeast-to-host tissue adherence and yeast aggregation. Plays an important role in the pathogenesis of C.albicans infections (PubMed:17510860, PubMed:22321066, PubMed:22429754). Allele ALS9-2 contributes to endothelial cell adhesion, whereas ALS9-1 does not (PubMed:17600078).<ref>PMID:17510860</ref> <ref>PMID:17600078</ref> <ref>PMID:22321066</ref> <ref>PMID:22429754</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Candida 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<ref>PMID:21896717</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2y7m" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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[[Category: Candida albicans]] | [[Category: Candida albicans]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Cota E]] |
| - | [[Category: | + | [[Category: Salgado PS]] |
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Current revision
Structure of N-terminal domain of Candida albicans als9-2 (Pt derivative)
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