Conserved water-mediated hydrogen bond network between TM-I, -II, -VI, and -VII in 7TM receptor activation.

ABSTRACT: Five highly conserved polar residues connected by a number of structural water molecules together with two rotamer micro-switches, TrpVI:13 and TyrVII:20, constitute an extended hydrogen bond network between the intracellular segments of TM-I, -II, -VI, and -VII of 7TM receptors. Molecular dynamics simulations showed that, although the fewer water molecules in rhodopsin were relatively movable, the hydrogen bond network of the beta2-adrenergic receptor was fully loaded with water molecules that were surprisingly immobilized between the two rotamer switches, both apparently being in their closed conformation. Manipulations of the rotamer state of TyrVII:20 and TrpVI:13 demonstrated that these residues served as gates for the water molecules at the intracellular and extracellular ends of the

SUBMITTER: Nygaard R 

PROVIDER: S-EPMC2885241 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature