MACEK, Pavel, Petr NOVÁK, Hana KŘÍŽOVÁ, Lukáš ŽÍDEK and Vladimír SKLENÁŘ. Molecular dynamics study of major urinary protein-pheromone interactions: A structural model for ligand-induced flexibility increase. FEBS Letters. Amsterdam: Elsevier Science B.V., 2006, vol. 580, No 1, p. 682-684. ISSN 0014-5793. |
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@article{701742, author = {Macek, Pavel and Novák, Petr and Křížová, Hana and Žídek, Lukáš and Sklenář, Vladimír}, article_location = {Amsterdam}, article_number = {1}, keywords = {Major urinary protein; Molecular dynamics simulation; Pheromone–protein interaction; Molecular motion; TZL; Order parameter}, language = {eng}, issn = {0014-5793}, journal = {FEBS Letters}, title = {Molecular dynamics study of major urinary protein-pheromone interactions: A structural model for ligand-induced flexibility increase}, url = {http://dx.doi.org/10.1016/j.febslet.2005.12.088}, volume = {580}, year = {2006} }
TY - JOUR ID - 701742 AU - Macek, Pavel - Novák, Petr - Křížová, Hana - Žídek, Lukáš - Sklenář, Vladimír PY - 2006 TI - Molecular dynamics study of major urinary protein-pheromone interactions: A structural model for ligand-induced flexibility increase JF - FEBS Letters VL - 580 IS - 1 SP - 682-684 EP - 682-684 PB - Elsevier Science B.V. SN - 00145793 KW - Major urinary protein KW - Molecular dynamics simulation KW - Pheromone–protein interaction KW - Molecular motion KW - TZL KW - Order parameter UR - http://dx.doi.org/10.1016/j.febslet.2005.12.088 N2 - 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. ER -
MACEK, Pavel, Petr NOVÁK, Hana KŘÍŽOVÁ, Lukáš ŽÍDEK and Vladimír SKLENÁŘ. Molecular dynamics study of major urinary protein-pheromone interactions: A structural model for ligand-induced flexibility increase. \textit{FEBS Letters}. Amsterdam: Elsevier Science B.V., 2006, vol.~580, No~1, p.~682-684. ISSN~0014-5793.
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