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Modeling and simulation of the human opioid receptor

¹ Department of Biochemistry and
² Department of Chemistry, Kansas State University, Manhattan, Kansas 66506, USA

(RECEIVED March 4, 2004; FINAL REVISION May 11, 2004; ACCEPTED May 11, 2004)

A model for the human opioid receptor has been generated via sequence alignment, structure building using the crystal structure of bovine rhodopsin as a template, and refinement by molecular dynamics simulation. The model building suggested that, in addition to the previously postulated interaction between D128 and Y308, an internal salt bridge also exists between residues D128 and R192, both of which are conserved in all the opioid receptors. The model and salt bridge were then shown to be stable during a 20-nsec simulation in a lipid bilayer. It is therefore proposed that both of these interactions play a role in stabilizing the inactive state of the receptor. The model is also used in an effort to rationalize many of the mutational studies performed on opioid receptors, and to suggest a plausible explanation for the differences between known opioid agonists and antagonists.

Keywords: molecular dynamics; bovine rhodopsin; GPCR; agonist-antagonist binding; activation mechanism

Reprint requests to: Paul E. Smith, Department of Chemistry, 111 Willard Hall, Kansas State University, Manhattan, KS 66506-3701, USA; e-mail: pesmith{at}ksu.edu; fax: (785) 532-6666.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.04720304.

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