Computational development of an alpha1A-adrenoceptor model in a membrane mimic.
A number of subtypes of the alpha-adrenoceptor have been identified; however, knowledge of the three-dimensional structures of such membrane proteins is limited, and no crystal structure of an alpha-adrenoceptor is available to date. We have developed and analysed homology models of the alpha1A-adrenoceptor subtype based on the bovine rhodopsin crystal structure (1l9 h). Subsequent structural refinement was performed through molecular dynamics simulations using the Amber 7 suite of programs with a biphasic H2O/CHCl3/H2O cell utilised to mimic the receptor's natural membrane environment.
Department of Chemistry, Trinity College Dublin, Dublin 2, Ireland.
Gemma K
GK
Kinsella
Isabel
I
Rozas
Graeme W
GW
Watson
D000818:Animals; D002417:Cattle; D019295:Computational Biology / Q000379:methods*; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D008968:Molecular Conformation; D011487:Protein Conformation; D017510:Protein Folding; D018340:Receptors, Adrenergic, alpha-1 / Q000737:chemistry*; D012243:Rhodopsin / Q000737:chemistry; D012984:Software
C547713:ADRA1A protein, human; D018340:Receptors, Adrenergic, alpha-1; D012243:Rhodopsin