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FEBS Lett

Title:		Molecular dynamics study of major urinary protein-pheromone interactions: a structural model for ligand-induced flexibility increase
Author(s):		Macek P; Novak P; Krizova H; Zidek L; Sklenar V;
Address:		"National Centre for Biomolecular Research, Faculty of Science, Masaryk University in Brno, Kotlarska 2, 611 37 Brno, Czech Republic"
Journal Title:		FEBS Lett
Year:		2006
Volume:		20060106
Issue:		2
Page Number:		682 - 684
DOI:		10.1016/j.febslet.2005.12.088
ISSN/ISBN:		0014-5793 (Print) 0014-5793 (Linking)
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"
Keywords:		"Computer Simulation Hydrogen Bonding *Models, Molecular Pheromones/chemistry/*metabolism Protein Isoforms/chemistry/metabolism *Protein Structure, Tertiary *Proteins/chemistry/metabolism;"
Notes:		"MedlineMacek, Pavel Novak, Petr Krizova, Hana Zidek, Lukas Sklenar, Vladimir eng Research Support, Non-U.S. Gov't England 2006/01/18 FEBS Lett. 2006 Jan 23; 580(2):682-4. doi: 10.1016/j.febslet.2005.12.088. Epub 2006 Jan 6"