703DSS: Difference between revisions

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The <scene name='71/716487/Extracellular_region/1'>extracellular region</scene> is relatively large compared to the other two regions, and contains a short C-terminus and a larger N-terminus. The N-terminus of the extracellular region is where the ligand binding occurs, and therefore deals with the agonists and antagonists. <ref>Perumal, R., & Mahesh, R. (2006). Synthesis and biological evaluation of a novel structural type of serotonin 5-HT3 receptor antagonists. Bioorganic & Medicinal Chemistry Letters, 2769-2772.</ref>  
The <scene name='71/716487/Extracellular_region/1'>extracellular region</scene> is relatively large compared to the other two regions, and contains a short C-terminus and a larger N-terminus. The N-terminus of the extracellular region is where the ligand binding occurs, and therefore deals with the agonists and antagonists. <ref>Perumal, R., & Mahesh, R. (2006). Synthesis and biological evaluation of a novel structural type of serotonin 5-HT3 receptor antagonists. Bioorganic & Medicinal Chemistry Letters, 2769-2772.</ref>  
These <scene name='71/716487/Binding_site/1'>binding sites</scene> are located between two bordering subunits, assembled from three alpha-helices of one subunit and three beta-strands from the other subunit. Such connection creates a binding pocket with a small, select number of residues from each subunit pointed into the binding pocket, as opposed to the large remainder of residues that are pointing away from the binding pocket. <ref>Hassaine, G., Deluz, C., Grasso, L., Wyss, R., Tol, M., Hovius, R., . . . Nury, H. (2014). X-ray  
These <scene name='71/716487/Binding_site/1'>binding sites</scene> are located between two bordering subunits, assembled from three alpha-helices of one subunit and three beta-strands from the other subunit. Such connection creates a binding pocket with a small, select number of residues from each subunit pointed into the binding pocket, as opposed to the large remainder of residues that are pointing away from the binding pocket. <ref>Hassaine, G., Deluz, C., Grasso, L., Wyss, R., Tol, M., Hovius, R., . . . Nury, H. (2014)</ref> X-ray  
structure of the mouse serotonin 5-HT3 receptor. Nature, 276-281.</ref> This binding pocket shrinks around agonists, encapsulating them, and widens around antagonists, repulsing them.  
structure of the mouse serotonin 5-HT3 receptor. Nature, 276-281.</ref> This binding pocket shrinks around agonists, encapsulating them, and widens around antagonists, repulsing them.