Informace o publikaci
Molecular dynamics study of major urinary protein-pheromone interactions: A structural model for ligand-induced flexibility increase
| Autoři | |
|---|---|
| Rok publikování | 2006 |
| Druh | Článek v odborném periodiku |
| Časopis / Zdroj | FEBS Letters |
| Fakulta / Pracoviště MU | |
| Citace | |
| www | http://dx.doi.org/10.1016/j.febslet.2005.12.088 |
| Obor | Biochemie |
| Klíčová slova | Major urinary protein; Molecular dynamics simulation; Pheromone–protein interaction; Molecular motion; TZL; Order parameter |
| Popis | Recently, two independent 15N 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 S2 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. |
| Související projekty: |