View source for 2ylh


==Structure of N-terminal domain of Candida albicans Als9-2 G299W mutant==
<StructureSection load='2ylh' size='340' side='right'caption='[[2ylh]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ylh]] 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=2YLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YLH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</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=2ylh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ylh OCA], [https://pdbe.org/2ylh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ylh RCSB], [https://www.ebi.ac.uk/pdbsum/2ylh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ylh 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ylh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Candida albicans]]
[[Category: Large Structures]]
[[Category: Burchell L]]
[[Category: Cota E]]
[[Category: Salgado PS]]