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Journal of Biomedicine and Biotechnology
Volume 2012 (2012), Article ID 789741, 12 pages
Research Article

Molecular Modeling of the M3 Acetylcholine Muscarinic Receptor and Its Binding Site

1Centre de Biotecnologia Molecular, Departament d’Enginyeria Química, Universitat Politècnica de Catalunya, 08028 Barcelona, Spain
2Centre de Biotecnologia Molecular, Departament d’Enginyeria Quimica, Universitat Politècnica de Catalunya, 08222 Terrassa, Spain
3Laboratori de Medicina Computacional, Unitat de Bioestadistica, Facultat de Medicina, Universitat Autonoma de Barcelona, 08193 Bellaterra, Spain

Received 19 July 2011; Accepted 8 November 2011

Academic Editor: Alejandro Giorgetti

Copyright © 2012 Marlet Martinez-Archundia et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Supplementary Material

Figure 1S. Forward and reverse primers for the mutants F222A and T235A.

Figure 2S. Root mean square fluctuations (rmsf) of Cα atoms, from an average structure computed from the last 25ns of the trajectories, were also calculated for the four trajectories.

Figure 3S. Definition of the dihedral angles of the antagonist NMS that were measured along the simulations.

Figure 4S. Values of the four dihedral angles of NMS measured in the different simulations: (a) POPC and (b) POPC/POPS.

Figure 5S. Representative Saturation Binding Curves of WT M3R and mutants F222A and T235A expressed in COS7 cells. The membranes were incubated with increasing concentrations of [3H] NMS in Hepes buffer at 30°C for about 2.5 hours. The protein concentration used was ca 10μg/mL. The specific and non-specific binding are expressed in fmol/mg protein.

  1. Supplementary Material