Juan A. Ballesteros

TL;DR: This chapter discusses the integrated methods for the construction of three-dimensional models and computational probing of structure–function relations in G protein-coupled receptors (GPCR) and expects increased rate of success achieved by molecular modeling and computational simulation methods in providing structural insights relevant to the functions of biological molecules.

TL;DR: Evidence for the existence of an ionic lock that constrains the relative mobility of the cytoplasmic ends of TM3 and TM6 in the inactive state of the β2-adrenergic receptor is provided and ionic interactions between Asp/Glu3.49, Arg3.50, and Glu6.30 may constitute a common switch governing the activation of many rhodopsin-like G-protein-coupled receptors.

TL;DR: In this paper, the crystal structures of both ground state and a photoactivated deprotonated intermediate of bovine rhodopsin at a resolution of 4.15 A were reported.

TL;DR: It is proposed that the overall structures of rhodopsin and of amine receptors are very similar, although there are also localized regions where the structure of these receptors may diverge.

TL;DR: Differential modulation of the accessibility of Cys (6.47) and an engineered Cys(6.52) in wild type and a constitutively active background provides experimental support for the association of this rotamer switch with receptor activation.