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Conference publicationsAbstractsXX conferenceFactors stabilizing the active state of β2-adrenergic receptor: MD studyMoscow State University, Faculty of Chemistry, Department of Physical Chemistry, Russia, 119991, Moscow, Leninskie gory, 1-3 1 pp. (accepted)Molecular dynamics simulations were used to study the influence of the interhelical hydrogen bonds and the cholesterol molecule on a stabilization of the β2-adrenergic receptor’s active state. β2-Adrenergic receptor (β2AR) is one of membrane proteins that transmit signals into the cell. Study of its spatial structure revealed the latent interhelical hydrogen bond between the hydroxyl group of Ser742.45 and the NH-group of Trp1584.50 indole ring [1]. We believe that this hydrogen bond is responsible for a stabilization of the active state of the β2 adrenergic receptor and for a promotion of cholesterol binding. Molecular dynamics studies of native and mutated β2 adrenergic receptor were performed by using the software package GROMACS. Proteins were embedded in a lipid bilayer according to the structure retrieved from the Orientations of Proteins in Membranes database. In order to eliminate the interhelical hydrogen bond, Ser742.45 residue was replaced by Ala742.45 in the mutated receptor structure. Two molecules β2AR and some cholesterol molecules were embedded in a lipid bilayer, as well as in the crystal structure of the protein (PDB ID: 2RH1). The calculations were performed on the “Lomonosov” supercomputer in the Moscow State University.
Preference. 1. Adamian L., Naveed H., Liang J. Lipid-Binding Surfaces of Membrane Proteins: Evidence from Evolutionary and Structural Analysis // Biochim. Biophys. Acta. V.1808, 2011. P.1092-1102.
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