Receptor: Difference between revisions

Line 19:

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>.

*[[Nicotinic Acetylcholine Receptor|Nicotinic Acetylcholine Receptors in general]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

Revision as of 07:59, 18 April 2021 view source Alexander Berchansky (talk \| contribs) 29,726 edits No edit summary ← Older edit		Revision as of 08:01, 18 April 2021 view source Alexander Berchansky (talk \| contribs) 29,726 edits No edit summary Newer edit →
Line 19:		Line 19:

	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 <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>.




	*[[Nicotinic Acetylcholine Receptor\|Nicotinic Acetylcholine Receptors in general]]		*[[Nicotinic Acetylcholine Receptor\|Nicotinic Acetylcholine Receptors in general]]