This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2y7l

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 04:29, 30 September 2022

Structure of N-terminal domain of Candida albicans Als9-2 in complex with human fibrinogen gamma peptide

Structural highlights

2y7l is a 2 chain structure with sequence from Candida albicans and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).^[1] ^[2] ^[3] ^[4]

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^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Klotz SA, Gaur NK, De Armond R, Sheppard D, Khardori N, Edwards JE Jr, Lipke PN, El-Azizi M. Candida albicans Als proteins mediate aggregation with bacteria and yeasts. Med Mycol. 2007 Jun;45(4):363-70. doi: 10.1080/13693780701299333. PMID:17510860 doi:http://dx.doi.org/10.1080/13693780701299333
↑ Zhao X, Oh SH, Hoyer LL. Unequal contribution of ALS9 alleles to adhesion between Candida albicans and human vascular endothelial cells. Microbiology (Reading). 2007 Jul;153(Pt 7):2342-2350. doi:, 10.1099/mic.0.2006/005017-0. PMID:17600078 doi:http://dx.doi.org/10.1099/mic.0.2006/005017-0
↑ Aoki W, Kitahara N, Miura N, Morisaka H, Kuroda K, Ueda M. Profiling of adhesive properties of the agglutinin-like sequence (ALS) protein family, a virulent attribute of Candida albicans. FEMS Immunol Med Microbiol. 2012 Jun;65(1):121-4. doi:, 10.1111/j.1574-695X.2012.00941.x. Epub 2012 Mar 6. PMID:22321066 doi:http://dx.doi.org/10.1111/j.1574-695X.2012.00941.x
↑ Monroy-Perez E, Sainz-Espunes T, Paniagua-Contreras G, Negrete-Abascal E, Rodriguez-Moctezuma JR, Vaca S. Frequency and expression of ALS and HWP1 genotypes in Candida albicans strains isolated from Mexican patients suffering from vaginal candidosis. Mycoses. 2012 May;55(3):e151-7. doi: 10.1111/j.1439-0507.2012.02188.x. Epub 2012 , Mar 19. PMID:22429754 doi:http://dx.doi.org/10.1111/j.1439-0507.2012.02188.x
↑ Salgado PS, Yan R, Taylor JD, Burchell L, Jones R, Hoyer LL, Matthews SJ, Simpson PJ, Cota E. Structural basis for the broad specificity to host-cell ligands by the pathogenic fungus Candida albicans. Proc Natl Acad Sci U S A. 2011 Sep 20;108(38):15775-9. Epub 2011 Sep 6. PMID:21896717 doi:10.1073/pnas.1103496108

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2y7l"

Categories: Candida albicans | Homo sapiens | Large Structures | Cota E | Salgado PS

@@ Line 3: / Line 3: @@
 <StructureSection load='2y7l' size='340' side='right'caption='[[2y7l]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2y7l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_11006_[[candida_stellatoidea]] Atcc 11006 [[candida stellatoidea]]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y7L FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2y7l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans Candida albicans] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y7L FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2y7n|2y7n]], [[2y7m|2y7m]], [[2y7o|2y7o]]</div></td></tr>
+</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=2y7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y7l OCA], [https://pdbe.org/2y7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y7l RCSB], [https://www.ebi.ac.uk/pdbsum/2y7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y7l ProSAT]</span></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=2y7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y7l OCA], [https://pdbe.org/2y7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y7l RCSB], [https://www.ebi.ac.uk/pdbsum/2y7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y7l 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 ==
@@ Line 23: / Line 24: @@
 __TOC__
 </StructureSection>
+[[Category: Candida albicans]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Cota, E]]
+[[Category: Cota E]]
-[[Category: Salgado, P S]]
+[[Category: Salgado PS]]
-[[Category: Adhesin]]
-[[Category: Cell adhesion]]
-[[Category: Peptide binding protein]]

2y7l

From Proteopedia

Revision as of 04:29, 30 September 2022

Structure of N-terminal domain of Candida albicans Als9-2 in complex with human fibrinogen gamma peptide

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox