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>

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> This binding pocket shrinks around agonists, encapsulating them, and widens around antagonists, repulsing them.

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 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 transmembrane region 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 (Hassaine ~~et al~~., 2014). M2, the porous domain, contains rings of charged amino acids at both its start and its end, accounting for M2’s main contribution to ion selectivity. The M3 and M4 alpha-helices create a large loop with one another, thus assembling the intracellular region (Barnes et al., 2009).

The transmembrane region 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> 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> M2, the porous domain, contains rings of charged amino acids at both its start and its end, accounting for M2’s main contribution to ion selectivity. The M3 and M4 alpha-helices create a large loop with one another, thus assembling the intracellular region (Barnes et al., 2009).

== Function ==

Line 53:

Thompson, A. J., & Lummis, S. C. R. (2006). 5-HT3 receptors. Current Pharmaceutical Design, 12(28), 3615–3630.

Barnes, N., Hales, T., Lummis, S., & Peters, J. (2009). The 5-HT3 receptor – the relationship between

structure and function. Neuropharmacology, 273-284.

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.

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.

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@@ Line 10: / Line 10: @@
 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)</ref> This binding pocket shrinks around agonists, encapsulating them, and widens around antagonists, repulsing them.
+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 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 transmembrane region 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 (Hassaine et al., 2014). M2, the porous domain, contains rings of charged amino acids at both its start and its end, accounting for M2’s main contribution to ion selectivity. The M3 and M4 alpha-helices create a large loop with one another, thus assembling the intracellular region (Barnes et al., 2009).
+The transmembrane region 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> 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> M2, the porous domain, contains rings of charged amino acids at both its start and its end, accounting for M2’s main contribution to ion selectivity. The M3 and M4 alpha-helices create a large loop with one another, thus assembling the intracellular region (Barnes et al., 2009).
 == Function ==
@@ Line 53: / Line 53: @@
 Thompson, A. J., & Lummis, S. C. R. (2006). 5-HT3 receptors. Current Pharmaceutical Design, 12(28), 3615–3630.
+Barnes, N., Hales, T., Lummis, S., & Peters, J. (2009). The 5-HT3 receptor – the relationship between
+structure and function. Neuropharmacology, 273-284.
+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.
+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.