Molecular dynamics study of major urinary protein-pheromone interactions: a structural model for ligand-induced flexibility increase
Language English Country Great Britain, England Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
16412435
DOI
10.1016/j.febslet.2005.12.088
PII: S0014-5793(05)01573-5
Knihovny.cz E-resources
- MeSH
- Pheromones chemistry metabolism MeSH
- Models, Molecular * MeSH
- Computer Simulation MeSH
- Protein Isoforms chemistry metabolism MeSH
- Proteins * chemistry metabolism MeSH
- Protein Structure, Tertiary * MeSH
- Hydrogen Bonding MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Pheromones MeSH
- major urinary proteins MeSH Browser
- Protein Isoforms MeSH
- Proteins * MeSH
Recently, two independent (15)N NMR relaxation studies indicated that in contrast to the decreased flexibility expected for induced-fit interactions, the backbone flexibility of major urinary protein isoform I (MUP-I) slightly increased upon complex formation with its natural pheromone 2-sec-butyl-4,5-dihydrothiazol. We have investigated the subtle details of molecular interactions by molecular dynamics simulations in explicit solvent. The calculated order parameters S(2) for a free- and ligand-bound protein supply evidence that mobility in various regions of MUP-I can be directly related to small conformational changes of the free- and complexed protein resulting from modifications of the hydrogen bonding network.
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