Automated method for modeling seven-helix transmembrane receptors from experimental data.
AUTOR(ES)
Herzyk, P
RESUMO
A rule-based automated method is presented for modeling the structures of the seven transmembrane helices of G-protein-coupled receptors. The structures are generated by using a simulated annealing Monte Carlo procedure that positions and orients rigid helices to satisfy structural restraints. The restraints are derived from analysis of experimental information from biophysical studies on native and mutant proteins, from analysis of the sequences of related proteins, and from theoretical considerations of protein structure. Calculations are presented for two systems. The method was validated through calculations using appropriate experimental information for bacteriorhodopsin, which produced a model structure with a root mean square (rms) deviation of 1.87 A from the structure determined by electron microscopy. Calculations are also presented using experimental and theoretical information available for bovine rhodopsin to assign the helices to a projection density map and to produce a model of bovine rhodopsin that can be used as a template for modeling other G-protein-coupled receptors.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1236480Documentos Relacionados
- Expression cloning of cDNA encoding a seven-helix receptor from human placenta with affinity for opioid ligands.
- Expression cloning of cDNA encoding a seven-helix receptor from human placenta with affinity for opioid ligands
- A molecular mechanism for signaling between seven-transmembrane receptors: evidence for a redistribution of G proteins
- Light-induced exposure of the cytoplasmic end of transmembrane helix seven in rhodopsin
- Computer-aided nucleic acid secondary structure modeling incorporating enzymatic digestion data.