title: Molecular dynamics study of major urinary protein-pheromone interactions: a structural model for ligand-induced flexibility increase.
abstract: 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.
authors.affiliation: National Centre for Biomolecular Research, Faculty of Science, Masaryk University in Brno, Kotlárská 2, 611 37 Brno, Czech Republic.
authors.forename: Pavel
authors.initials: P
authors.lastname: Macek
authors.forename: Petr
authors.initials: P
authors.lastname: Novák
authors.forename: Hana
authors.initials: H
authors.lastname: Krízová
authors.forename: Lukás
authors.initials: L
authors.lastname: Zídek
authors.forename: Vladimír
authors.initials: V
authors.lastname: Sklenár
mesh_terms: D003198:Computer Simulation; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010675:Pheromones / Q000737:chemistry / Q000378:metabolism*; D020033:Protein Isoforms / Q000737:chemistry / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D010675:Pheromones; D020033:Protein Isoforms; D011506:Proteins; C035737:major urinary proteins