Molecular dynamics study of major urinary protein-pheromone interactions: A structural model for ligand-induced flexibility increase

• Autoři: MACEK Pavel; NOVÁK Petr; KŘÍŽOVÁ Hana; ŽÍDEK Lukáš; SKLENÁŘ Vladimír
• Rok publikování: 2006
• Druh: Článek v odborném periodiku
• Časopis / Zdroj: FEBS Letters
• Fakulta / Pracoviště MU: Přírodovědecká fakulta
• 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

• Proteiny v metabolismu a při interakci organismů s prostředím
• Biomolekulární centrum
• Strukturně-funkční vztahy biomolekul a jejich role v metabolismu