To the best of our knowledge so far [29,32,38,39,42,43,46,47,48,49,50,51], two MCHR1 binding pockets (listed as P1 and P2, respectively) have been proposed. P1 represents the conventional binding cavity that almost all docking researches have referred to where a typical interaction of salt bridge is found experimentally formed by Asp123, and simultaneously H-bond or hydrophobic regions may also be embodied. Crucial residues of P1 are composed of Phe213, Phe217, Gln212, Tyr272, Tyr273, Tyr293, Tyr301, Gln276, Gln127 besides Asp123. An elaborated discussion of the binding mode of P1 is provided later. With regard to P2, it was only introduced by Abu-Hammad et al. [49] in 2009. Unlike those in P1, binding forces in P2 contain van der Waals stacking instead of ionic interaction in addition to the hydrophobic effect and H-bond. As noticed in the arrangement of residues around P2 depicted in Figure 10A, crucial amino acids consist of Leu184, Ile185, Phe187, Pro199, Leu205, Thr209, Gln212, Leu280, Arg284 and Gln276, from which we infer that the location of P2 borders to that of P1 with common residues Gln212 and Gln276. These two residues participate in the interaction with MCHR1 antagonists as well forming hydrogen bonds. A van der Waals stacking between the phenyl moiety and Phe187 was also observed. The visualized positions of both cavities are illustrated in Figure 11.
X Force Keygen Character Generator 2009 Activation
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