Modeling of G-protein coupled receptors with bacteriorhodopsin as a template. A novel approach based on interaction energy differences.
The structure of bacteriorhodopsin was used as a template to generate a model for G-protein coupled receptors. However, these receptors and the template are not related by sequence homology. Therefore a pragmatic and reproducible approach was developed to achieve an energetically favourable accommodation of receptor sequences to the backbone structure of bacteriorhodopsin. Improved interaction energy differences are used in a two step procedure analogous to a hypothetical folding mechanism for integral membrane proteins. The resulting model is in good agreement with existing data from structure-function studies.
Röper
D
D
Institut für Biochemie, Rheinisch-Westfälische Technische Hochschule Aachen, Germany.
Jacoby
E
E
Krüger
P
P
Engels
M
M
Grötzinger
J
J
Wollmer
A
A
Strassburger
W
W
D000595:Amino Acid Sequence; D000818:Animals; D001436:Bacteriorhodopsins / Q000737:chemistry*; D002417:Cattle; D019204:GTP-Binding Proteins / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D044087:Receptor, Anaphylatoxin C5a; D018343:Receptors, Adrenergic, beta-2 / Q000737:chemistry*; D011951:Receptors, Complement / Q000737:chemistry*
D044087:Receptor, Anaphylatoxin C5a; D018343:Receptors, Adrenergic, beta-2; D011951:Receptors, Complement; D001436:Bacteriorhodopsins; D019204:GTP-Binding Proteins