Structural and Functional Analysis of the Tandem β-Zipper Interaction of a Streptococcal Protein with Human Fibronectin

Bacterial fibronectin-binding proteins (FnBPs) contain a large intrinsically disordered region (IDR) that mediates adhesion of bacteria to host tissues, and invasion of host cells, through binding to fibronectin (Fn). These FnBP IDRs consist of Fn-binding repeats (FnBRs) that form a highly extended...

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Veröffentlicht in:	The Journal of biological chemistry 2011-11, Vol.286 (44), p.38311-38320
Hauptverfasser:	Norris, Nicole C., Bingham, Richard J., Harris, Gemma, Speakman, Adrian, Jones, Richard P.O., Leech, Andrew, Turkenburg, Johan P., Potts, Jennifer R.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adhesins, Bacterial - chemistry Adhesins, Bacterial - metabolism Calorimetry Crystallography, X-Ray - methods Fibronectin Fibronectins - chemistry Host-Pathogen Interactions Humans Isothermal Titration Calorimetry Kinetics Magnetic Resonance Spectroscopy - methods Markov Chains Molecular Conformation Mutagenesis, Site-Directed Mutation Protein Binding Protein Complexes Protein Conformation Protein Structure Protein Structure and Folding Protein-Protein Interactions Streptococcus pyogenes - metabolism Surface Plasmon Resonance Thermodynamics
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