Opioid receptors computational models

Based on the experimental data, a computational model of OFQ/N bound to ORLl receptors has been proposed (189). In this model the N-terminal sequence containing the two Phe residues binds in a highly conserved pocket formed by TM3, 5, 6, and 7, which is similar to that proposed for opioid receptors. Residues 5-7 (Thr-Gly-Ala) of OFQ/N are then positioned at the TM-EL2 interface in a largely nonconserved region unfavorable side-chain interactions in this region of the receptor are then used to explain the selectivity of the ORLl receptor for OFQ/N over Dyn A. The positively charged C-terminus of the peptide is proposed to make multiple contacts with the highly acidic EL2. 

University of Minnesota Center for Opioid Research and Design (CORD), http //www. opioid.umn.edu. This site includes computational models of the opioid receptors, a complete list of chimeric receptors and point mutations in opioid receptors with pharmacological data and literature references, and links to other relevant sites. 

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