Sandbox Reserved 1449: Difference between revisions

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== Structural highlights ==

The molecular structure of MOR-1 was better understood after its cloning in 1993. According to the American Society for Pharmacology and Experimental Therapeutics, the amino acid sequence of MOR-1 is 60-70% homologous to the other classes of opioid receptors. The difference between MOR-1 and the other opioid receptor proteins lies in its extracellular N-terminus, intracellular C-terminus, and second and third extracellular loops. The μ-opioid receptor is a<scene name='77/778329/7tm/1'> 7-multispanning integral membrane protein</scene> found in dorsal root ganglion cells and peripheral nerve cells in humans, with its binding site exposed to the extracellular surface. The transmembrane domain of MOR-1 will dimerize at TM5 and TM6 to form oligomers. <ref name= "Article 1" >Pasternak, G. W., and Y.-X. Pan. “Mu Opioids and Their Receptors: Evolution of a Concept.” Pharmacological Reviews, vol. 65, no. 4, 2013, pp. 1257–1317., doi:10.1124/pr.112.007138. </ref>. The active site of the receptor, where opioid molecules bind, is between TM3, TM5, TM6, and TM7.

The molecular structure of MOR-1 was better understood after its cloning in 1993. According to the American Society for Pharmacology and Experimental Therapeutics, the amino acid sequence of MOR-1 is 60-70% homologous to the other classes of opioid receptors. The difference between MOR-1 and the other opioid receptor proteins lies in its extracellular N-terminus, intracellular C-terminus, and second and third extracellular loops. The μ-opioid receptor is a<scene name='77/778329/7tm/1'> 7-multispanning integral membrane protein</scene> found in dorsal root ganglion cells and peripheral nerve cells in humans, with its binding site exposed to the extracellular surface. The transmembrane domain of MOR-1 will dimerize at TM5 and TM6 to form oligomers. <ref name= "Article 1" >Pasternak, G. W., and Y.-X. Pan. “Mu Opioids and Their Receptors: Evolution of a Concept.” Pharmacological Reviews, vol. 65, no. 4, 2013, pp. 1257–1317., doi:10.1124/pr.112.007138. </ref>. The active site of the receptor, where opioid molecules bind, is between TM3, TM5, TM6, and TM7. <ref name= "Article 2" >Serohijos, Adrian W.r., et al. “Structural Basis for μ-Opioid Receptor Binding and Activation.” Structure, vol. 19, no. 11, 9 Nov. 2011, pp. 1683–1690., doi:10.1016/j.str.2011.08.003. </ref>.

== Function ==

Sandbox Reserved 1449: Difference between revisions

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 == Structural highlights ==
-The molecular structure of MOR-1 was better understood after its cloning in 1993. According to the American Society for Pharmacology and Experimental Therapeutics, the amino acid sequence of MOR-1 is 60-70% homologous to the other classes of opioid receptors. The difference between MOR-1 and the other opioid receptor proteins lies in its extracellular N-terminus, intracellular C-terminus, and second and third extracellular loops. The μ-opioid receptor is a<scene name='77/778329/7tm/1'> 7-multispanning integral membrane protein</scene> found in dorsal root ganglion cells and peripheral nerve cells in humans, with its binding site exposed to the extracellular surface. The transmembrane domain of MOR-1 will dimerize at TM5 and TM6 to form oligomers. <ref name= "Article 1" >Pasternak, G. W., and Y.-X. Pan. “Mu Opioids and Their Receptors: Evolution of a Concept.” Pharmacological Reviews, vol. 65, no. 4, 2013, pp. 1257–1317., doi:10.1124/pr.112.007138. </ref>. The active site of the receptor, where opioid molecules bind, is between TM3, TM5, TM6, and TM7.
+The molecular structure of MOR-1 was better understood after its cloning in 1993. According to the American Society for Pharmacology and Experimental Therapeutics, the amino acid sequence of MOR-1 is 60-70% homologous to the other classes of opioid receptors. The difference between MOR-1 and the other opioid receptor proteins lies in its extracellular N-terminus, intracellular C-terminus, and second and third extracellular loops. The μ-opioid receptor is a<scene name='77/778329/7tm/1'> 7-multispanning integral membrane protein</scene> found in dorsal root ganglion cells and peripheral nerve cells in humans, with its binding site exposed to the extracellular surface. The transmembrane domain of MOR-1 will dimerize at TM5 and TM6 to form oligomers. <ref name= "Article 1" >Pasternak, G. W., and Y.-X. Pan. “Mu Opioids and Their Receptors: Evolution of a Concept.” Pharmacological Reviews, vol. 65, no. 4, 2013, pp. 1257–1317., doi:10.1124/pr.112.007138. </ref>. The active site of the receptor, where opioid molecules bind, is between TM3, TM5, TM6, and TM7. <ref name= "Article 2" >Serohijos, Adrian W.r., et al. “Structural Basis for μ-Opioid Receptor Binding and Activation.” Structure, vol. 19, no. 11, 9 Nov. 2011, pp. 1683–1690., doi:10.1016/j.str.2011.08.003. </ref>.
 == Function ==