Receptor: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 16: | Line 16: | ||
The <scene name='71/716487/Extracellular_region/1'>extracellular region</scene> is relatively large compared to the other 2 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. | The <scene name='71/716487/Extracellular_region/1'>extracellular region</scene> is relatively large compared to the other 2 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. | ||
These <scene name='71/716487/Binding_site/4'>binding sites</scene> are located between 2 bordering subunits, assembled from 3 α-helices of 1 subunit and 3 β-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 | These <scene name='71/716487/Binding_site/4'>binding sites</scene> are located between 2 bordering subunits, assembled from 3 α-helices of 1 subunit and 3 β-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. 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 4 | The <scene name='71/716487/Default/5'>transmembrane region</scene> is within the C-terminus region, and contains 4 α-helical domains within it (M1-M4) that stretch the length of this inner, transmembrane area. These 4 α-helical domains conduct the channel openings via ion selectivity, depending on both charge and size. 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 α-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>. | ||
'''The extracellular subunit interface of the 5-HT3 receptors: a computational alanine scanning mutagenesis study<ref>DOI 10.1080/07391102.2012.680029</ref>''' | '''The extracellular subunit interface of the 5-HT3 receptors: a computational alanine scanning mutagenesis study<ref>DOI 10.1080/07391102.2012.680029</ref>''' | ||
