Importance of oligomerisation on Pseudomonas aeruginosaLectin-II binding affinity. In silico and in vitro mutagenesis
Language English Country Germany Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Adhesins, Bacterial chemistry genetics metabolism MeSH
- Escherichia coli genetics MeSH
- Fucose chemistry metabolism MeSH
- Calorimetry methods MeSH
- Kinetics MeSH
- Binding, Competitive MeSH
- Crystallization MeSH
- Protein Structure, Quaternary MeSH
- Lectins chemistry genetics metabolism MeSH
- Models, Molecular MeSH
- Protein Multimerization MeSH
- Mutation * MeSH
- Computer Simulation MeSH
- Pseudomonas aeruginosa genetics metabolism MeSH
- Recombinant Proteins chemistry metabolism MeSH
- Sequence Deletion MeSH
- Protein Structure, Tertiary MeSH
- Thermodynamics MeSH
- Protein Binding MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- adhesin, Pseudomonas MeSH Browser
- Adhesins, Bacterial MeSH
- Fucose MeSH
- Lectins MeSH
- Recombinant Proteins MeSH
The effect of terminal GLY114* deletion on the binding affinity of the PA-IIL lectin toward L: -fucose was investigated. Both experimental (isothermal titration calorimetry) and computational (molecular dynamics simulations) methods have shown that the deletion mutation decreases the L-fucose affinity. It implies that the PA-IIL saccharide binding affinity is influenced by the dimerization of the lectin. A detailed analysis of computational data confirms the key role of electrostatic interactions in the PA-IIL/saccharide binding.
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