Sandbox Reserved 1646: Difference between revisions
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A detailed interaction network for elagolix has been described<ref>DOI: 10.1038/s41467-020-19109-w</ref> in which the N-terminus, residue Y283 and a polar <scene name='86/868179/Interacton-elox/2'>interaction network</scene> formed by residues D98 and K121 are of particular importance for ligand recognition. | A detailed interaction network for elagolix has been described<ref>DOI: 10.1038/s41467-020-19109-w</ref> in which the N-terminus, residue Y283 and a polar <scene name='86/868179/Interacton-elox/2'>interaction network</scene> formed by residues D98 and K121 are of particular importance for ligand recognition. | ||
'''<scene name='86/868179/N-terminus/ | '''<scene name='86/868179/N-terminus/3'>N terminus</scene>:''' fits in cavity (contact to surrounding residues: N102, Q174, and F178 from TM2 and TM4) indicating a distinct roles in mediating binding of different ligands. However, it is not engaged in GnRH activation of wild-type GnRH1R. | ||
'''<scene name='86/868179/Binding_pocket_bottem/1'>Y283:</scene>''' engaged in the ligand recognition and activation of GnRH1R29 together with Y284 and M125 are suggested to form the bottom wall | '''<scene name='86/868179/Binding_pocket_bottem/1'>Y283:</scene>''' engaged in the ligand recognition and activation of GnRH1R29 together with Y284 and M125 are suggested to form the bottom wall | ||
