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 name="perumal">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 <scene name='71/716487/Default/11'> away</scene> from the binding pocket<ref name="hassaine">Hassaine, G., Deluz, C., Grasso, L., Wyss, R., Tol, M., Hovius, R., . . . Nury, H. (2014). 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.

These <scene name='71/716487/Binding_site/4'>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 <scene name='71/716487/Default/11'> away</scene> from the binding pocket<ref name="hassaine">Hassaine, G., Deluz, C., Grasso, L., Wyss, R., Tol, M., Hovius, R., . . . Nury, H. (2014). 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.

The <scene name='71/716487/Default/5'>transmembrane region</scene> is within the C-terminus region, and contains four alpha-helical domains within it (M1-M4) that stretch the length of this inner, transmembrane area. These four alpha-helical domains conduct the channel openings via ion selectivity, depending on both charge and size<ref name="hassaine" />. M2, the porous domain, contains rings of charged amino acids at both its start and its <scene name='71/716487/Default/10'>end</scene>, accounting for M2’s main contribution to ion selectivity. The M3 and M4 alpha-helices create a large <scene name='71/716487/Default/6'> loop</scene> with one another, thus assembling the <scene name='71/716487/Default/7'>intracellular region</scene><ref name="barnes" />.

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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 name="perumal">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 <scene name='71/716487/Default/11'> away</scene> from the binding pocket<ref name="hassaine">Hassaine, G., Deluz, C., Grasso, L., Wyss, R., Tol, M., Hovius, R., . . . Nury, H. (2014). 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.
+These <scene name='71/716487/Binding_site/4'>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 <scene name='71/716487/Default/11'> away</scene> from the binding pocket<ref name="hassaine">Hassaine, G., Deluz, C., Grasso, L., Wyss, R., Tol, M., Hovius, R., . . . Nury, H. (2014). 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.
 The <scene name='71/716487/Default/5'>transmembrane region</scene> is within the C-terminus region, and contains four alpha-helical domains within it (M1-M4) that stretch the length of this inner, transmembrane area. These four alpha-helical domains conduct the channel openings via ion selectivity, depending on both charge and size<ref name="hassaine" />. M2, the porous domain, contains rings of charged amino acids at both its start and its <scene name='71/716487/Default/10'>end</scene>, accounting for M2’s main contribution to ion selectivity. The M3 and M4 alpha-helices create a large <scene name='71/716487/Default/6'> loop</scene> with one another, thus assembling the <scene name='71/716487/Default/7'>intracellular region</scene><ref name="barnes" />.