Predicting the Pose of β-Casomorphin-5 and 7 in the Opioid Receptors
Contribuinte(s) |
Department of Chemistry |
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Data(s) |
07/07/2015
07/07/2015
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Resumo |
The opioid receptors consist of three main subtypes; μ, δ, and κ. Previous binding studies have shown that fragments of the milk protein, β-casein, known as β-casomorphins are agonists of these receptors which are selective for the μ receptor subtype. Using the crystal structures of these three receptors, computational molecular docking studies were done using the software GOLD to determine the conformation of β-casomorphin-5 and 7 when they bind to these three opioid receptors. GOLD was able to discriminate among the three receptors when docking the rigid ligands co-crystalized with the receptors. However, GOLD could not discriminate among the three receptors for either of the highly flexible β-casomorphins. A per amino acid scoring method was developed to overcome this problem. This method was used to predict the conformation of both β-casomorphin-5 and 7 in the μ receptor and determine that the two amino acid residues, Lys303 and Trp318 of the μ receptor are responsible for discriminating among the three receptor subtypes for binding of the β-casomorphin-5 and 7. |
Identificador | |
Idioma(s) |
eng |
Publicador |
Brock University |
Palavras-Chave | #Opioid Receptors #β-Casomorphins #Computational Docking #Pose |
Tipo |
Electronic Thesis or Dissertation |