title: hβ2R-Gαs complex: prediction versus crystal structure--how valuable are predictions based on molecular modeling studies?
abstract: In 2010, we predicted two models for the hβ(2)R-Gα(s) complex by combining the technique of homology modeling with a potential energy surface scan, since a complete crystal structure of the hβ(2)R-Gα(s) complex was not available. The crystal structure of opsin co-crystallized with part of the C-terminus of Gα (3DQB) was used as a template to model the hβ(2)R, whereas the crystal structure of Gα (1AZT) was used as a template to model Gα(s). Utilizing a potential energy surface scan between hβ(2)R and Gα(s), a six-dimensional potential energy surface was obtained. Two significant minimum regions were located on this surface, and each was associated with a distinct hβ(2)R-Gα(s) complex, namely model I and model II [Straßer A, Wittmann H-J (2010) J Mol Model 16:1307-1318]. The crystal structure of the hβ(2)R-Gα(s)βγ complex has recently been published. Thus, the aim of the current study was, on the one hand, to compare our predicted structures with the true crystal structure, and on the other to discuss the question: how valuable are predictions based on molecular modeling studies?
authors.affiliation: Department of Pharmaceutical and Medicinal Chemistry II, Faculty of Chemistry and Pharmacy, University of Regensburg, Universitätsstraße 31, 93040 Regensburg, Germany. andrea.strasser@chemie.uni-regensburg.de
authors.forename: Andrea
authors.initials: A
authors.lastname: Straßer
authors.forename: Hans-Joachim
authors.initials: HJ
authors.lastname: Wittmann
mesh_terms: D044385:GTP-Binding Protein alpha Subunits / Q000737:chemistry*; D008958:Models, Molecular; D046912:Multiprotein Complexes / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D018343:Receptors, Adrenergic, beta-2 / Q000737:chemistry*; D015203:Reproducibility of Results
chemical_list: D044385:GTP-Binding Protein alpha Subunits; D046912:Multiprotein Complexes; D018343:Receptors, Adrenergic, beta-2