Molecular dynamics study of major urinary protein-pheromone interactions: a structural model for ligand-induced flexibility increase.
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.
Macek
Pavel
P
National Centre for Biomolecular Research, Faculty of Science, Masaryk University in Brno, Kotlárská 2, 611 37 Brno, Czech Republic.
Novák
Petr
P
Krízová
Hana
H
Zídek
Lukás
L
Sklenár
Vladimír
V
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
D010675:Pheromones; D020033:Protein Isoforms; D011506:Proteins; C035737:major urinary proteins