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The Peptide-binding Cavity Is Essential for Als3-mediated Adhesion of Candida albicans to Human Cells

DOI: 10.1074/jbc.M114.547877 DOI Help
PMID: 24802757 PMID Help

Authors: J. Lin (Department of Life Sciences, Imperial College London, U.K.) , S-h. Oh (Department of Pathobiology, University of Illinois Urbana-Champaign, USA) , Rhian Jones (Department of Life Sciences, Imperial College London, U.K.) , James Garnett (Department of Life Sciences, Imperial College London, U.K.) , Paula Salgado (Institute for Cell and Molecular Biosciences, Newcastle University, U.K.) , S. Rusnakova (Department of Life Sciences, Imperial College London, U.K.) , S. J. Matthews (Department of Life Sciences, Imperial College London, U.K.) , L. L. Hoyer (Department of Pathobiology, University of Illinois Urbana-Champaign, USA) , E. Cota (Department of Life Sciences, Imperial College London, U.K.)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Biological Chemistry , VOL 289 (26) , PAGES 18401 - 18412

State: Published (Approved)
Published: June 2014
Diamond Proposal Number(s): 9424

Open Access Open Access

Abstract: Adhesion; Aggregation; Als Adhesins; Candida albicans; Functional Amyloid; Nuclear Magnetic Resonance (NMR); Peptide-binding Cavity; Peptide-binding Protein; X-ray Crystallography

Journal Keywords: Candidiasis ; Crystallography ; X-Ray ; Endothelial; Fungal; Humans ; Models ; Molecular ; Protein; Tertiary

Subject Areas: Biology and Bio-materials


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength) , I24-Microfocus Macromolecular Crystallography