Human μ Opioid Receptor Models with Evaluation of the Accuracy Using the Crystal Structure of the Murine μ Opioid Receptor

Journal of Anesthesia & Clinical Research
Jose Manuel Perez-AguilarRenyu Liu

Abstract

Models of the human μ opioid receptor were constructed using available G-protein-coupled receptor (GPCR) structures using homology (comparative) modeling techniques. The recent publication of a high-resolution crystal structure of a construct based on the murine μ opioid receptor offers a unique opportunity to evaluate the reliability of the homology models and test the relevance of introducing more templates (known structures) to increase the accuracy of the comparative models. In the first model two templates were used: the β2 adrenergic and bovine rhodopsin receptors. For the second model, four templates were utilized: the β2 adrenergic, bovine rhodopsin, β1 adrenergic, and A2A adenosine receptors. Including additional templates improved the accuracy of structural motifs and other features of the model when the same sequence alignment was used. The predicted structures were especially relevant in the case of important receptor regions such as the DRY motif, which has been associated with receptor activation. Additionally, this study showed that receptor sequence similarity is crucial in homology modeling, as indicated in the case of the highly diverse EC2 loop. This study demonstrates the reliability of the homology modeling...Continue Reading

Citations

Jan 1, 2013·Computational and Structural Biotechnology Journal·Valère LounnasNicolas Foloppe
Jun 30, 2021·The Journal of Pharmacology and Experimental Therapeutics·Todd M HillhouseJohn R Traynor

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Methods Mentioned

BETA
X-ray

Software Mentioned

NAMD2
hMOP
STRIDE
Blosum62
Molprobity
PyMOL
R
ClustalW
Phyre
Modeller

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