703DSS: Difference between revisions

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The 5-HT3 receptor is bullet-shaped and consists of five subunits (A-E) that form an oligomer. In the center of this pentamer of subunits is a ligand-gated ion channel full of water, which the five subunits enclose pseudo-symmetrically. Each subunit of the 5-HT3 receptor consists of three regions; the extracellular region, the transmembrane region, and the intracellular region (Barnes et al., 2009).

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 (Perumal & Mahesh, 2006). These binding sites 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 (Hassaine et al., 2014). This binding pocket shrinks around agonists, encapsulating them, and widens around antagonists, repulsing them.

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 (Perumal & Mahesh, 2006). 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 (Hassaine et al., 2014). 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).

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@@ Line 7: / Line 7: @@
 The 5-HT3 receptor is bullet-shaped and consists of five subunits (A-E) that form an oligomer. In the center of this pentamer of subunits is a ligand-gated ion channel full of water, which the five subunits enclose pseudo-symmetrically. Each subunit of the 5-HT3 receptor consists of three regions; the extracellular region, the transmembrane region, and the intracellular region (Barnes et al., 2009).
-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 (Perumal & Mahesh, 2006). These binding sites 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 (Hassaine et al., 2014). This binding pocket shrinks around agonists, encapsulating them, and widens around antagonists, repulsing them.
+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 (Perumal & Mahesh, 2006). 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 (Hassaine et al., 2014). 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).