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4lee

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Revision as of 06:01, 5 August 2016

Structure of the Als3 adhesin from Candida albicans, residues 1-313 (mature sequence), triple mutant in the binding cavity: K59M, A116V, Y301F

Structural highlights

4lee is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	4le8, 4leb
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ALS3_CANAX] 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. Necessary for C.albicans to bind to N-cadherin on endothelial cells and E-cadherin on oral epithelial cells and subsequent endocytosis by these cells (By similarity).

Publication Abstract from PubMed

The adhesive phenotype of Candida albicans contributes to its ability to colonize the host and cause disease. Als proteins are one of the most widely studied C. albicans virulence attributes; deletion of ALS3 produces the greatest reduction in adhesive function. Although adhesive activity is thought to reside within the N-terminal domain of Als proteins (NT-Als), the molecular mechanism of adhesion remains unclear. We designed mutations in NT-Als3 that test the contribution of the peptide-binding cavity (PBC) to C. albicans adhesion, and assess the adhesive properties of other NT-Als3 features in the absence of a functional PBC. Structural analysis of purified loss-of-PBC-function mutant proteins showed that the mutations did not alter the overall structure or surface properties of NT-Als3. The mutations were incorporated into full-length ALS3 and integrated into the ALS3 locus of a deletion mutant, under control of the native ALS3 promoter. PBC-mutant phenotype was evaluated in assays using monolayers of human pharyngeal epithelial (FaDu) and umbilical vein endothelial (HUVEC) cells, and freshly collected human buccal epithelial cells (BEC) in suspension. Loss of PBC function resulted in an adhesion phenotype that was indistinguishable from the deltaals3/deltaals3 strain. The adhesive contribution of the Als3 amyloid-forming-region (AFR) was also tested using these methods. C. albicans strains producing cell-surface Als3 in which the amyloidogenic potential was destroyed, showed little contribution of the AFR to adhesion, instead suggesting an aggregative function for the AFR. Collectively, these results demonstrate the essential and principal role of the PBC in Als3 adhesion.

The Peptide-Binding Cavity is Essential for Als3-mediated Adhesion of Candida albicans to Human Cells.,Lin J, Oh SH, Jones R, Garnett JA, Salgado PS, Rusnakova S, Matthews S, Hoyer LL, Cota E J Biol Chem. 2014 May 6. pii: jbc.M114.547877. PMID:24802757^[1]

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

References

↑ Lin J, Oh SH, Jones R, Garnett JA, Salgado PS, Rusnakova S, Matthews S, Hoyer LL, Cota E. The Peptide-Binding Cavity is Essential for Als3-mediated Adhesion of Candida albicans to Human Cells. J Biol Chem. 2014 May 6. pii: jbc.M114.547877. PMID:24802757 doi:http://dx.doi.org/10.1074/jbc.M114.547877

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4lee"

@@ Line 1: / Line 1: @@
 ==Structure of the Als3 adhesin from Candida albicans, residues 1-313 (mature sequence), triple mutant in the binding cavity: K59M, A116V, Y301F==
 <StructureSection load='4lee' size='340' side='right' caption='[[4lee]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[4lee]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LEE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LEE FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4le8|4le8]], [[4leb|4leb]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lee OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lee RCSB], [http://www.ebi.ac.uk/pdbsum/4lee PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lee OCA], [http://pdbe.org/4lee PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lee RCSB], [http://www.ebi.ac.uk/pdbsum/4lee PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lee ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4lee" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4lee

From Proteopedia

Revision as of 06:01, 5 August 2016

Structure of the Als3 adhesin from Candida albicans, residues 1-313 (mature sequence), triple mutant in the binding cavity: K59M, A116V, Y301F

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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