Active state-like conformational elements in the beta2-AR and a photoactivated intermediate of rhodopsin identified by dynamic properties of GPCRs.
G-Protein-coupled receptors (GPCRs) adopt various functionally relevant conformational states in cell signaling processes. Recently determined crystal structures of rhodopsin and the beta 2-adrenergic receptor (beta 2-AR) offer insight into previously uncharacterized active conformations, but the molecular states of these GPCRs are likely to contain both inactive and active-like conformational elements. We have identified conformational rearrangements in the dynamics of the TM7-HX8 segment that relate to the properties of the conserved NPxxY(x)5,6F motif and show that they can be used to identify active state-like conformational elements in the corresponding regions of the new structures of rhodopsin and the beta 2-AR.
Department of Physiology and Biophysics, Weill Medical College, Cornell University, 1300 York Avenue, New York, New York 10021, USA.
Daniel S
DS
Han
Simon X
SX
Wang
Harel
H
Weinstein
D019943:Amino Acid Substitution; D003198:Computer Simulation; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D011487:Protein Conformation; D018343:Receptors, Adrenergic, beta-2 / Q000737:chemistry* / Q000378:metabolism; D043562:Receptors, G-Protein-Coupled / Q000737:chemistry / Q000378:metabolism*; D012243:Rhodopsin / Q000737:chemistry* / Q000378:metabolism
D018343:Receptors, Adrenergic, beta-2; D043562:Receptors, G-Protein-Coupled; D012243:Rhodopsin