Stratification of the channel domain in neurotransmitter receptors
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Cited by (76)
Neuronal Nicotinic Acetylcholine Receptor Structure and Function and Response to Nicotine
2015, International Review of NeurobiologyCitation Excerpt :Similarly, replacement of the α7 leucine at the extracellular entrance to the pore by threonine dramatically reduces the calcium permeability. However, substitution of the leucine by threonine at another polar ring of amino acids within the pore (position 247) did not alter divalent ionic selectivity, but altered agonist/antagonist relationships and aspects of desensitization (Bertrand et al., 1993a; Revah et al., 1991). These data illustrate the importance of particular conserved amino acids and the complex relationship between the structure of the pore and the resulting function.
What we have learned from crystal structures of proteins to receptor function
2011, Biochemical PharmacologyMicrosecond simulations indicate that ethanol binds between subunits and could stabilize an open-state model of a glycine receptor
2011, Biophysical JournalCitation Excerpt :The narrowest part of the pore was defined by the hydrophobic ring of L9′ (L261 in GlyRα1 sequence numbering) with a pore radius of 1.4 Å. This part of the pore, also called the equatorial leucine ring, was previously identified as a key element for ion gating (28). Since then, numerous works, including MD simulations, have shown the efficiency of the hydrophobic barrier for preventing ion permeation.
Alpha 7 nicotinic acetylcholine receptors: Molecular pharmacology and role in neuroprotection
2008, Current Anaesthesia and Critical CareCitation Excerpt :When the five α7 nAChR subunits come together to form a homopentameric ion channel, the central ion channel is mostly composed of the five α-helix-folded MSR II arranged symmetrically around an axis perpendicular to the membrane. The MSR II central core is supported by the other three MSR's in what appears to be a configuration resembling a ‘starfish’.85,88–90 In keeping with the ‘starfish’ analogy, the MSR IV α-helix forms the outside tip of a single pointed arm; the adjoining α-helix-turn-β-sheet MSR III and the β-sheet MSR I from the same peptide form the base of each arm surrounding the MSR II core channel.85,90,91
An energy-efficient gating mechanism in the acetylcholine receptor channel suggested by molecular and Brownian dynamics
2006, Biophysical JournalCitation Excerpt :Unwin initially suggested that the gate was located midway along the M2 helix where a number of conserved hydrophobic leucine and valine residues line the pore (5,10). Mutagenesis studies reveal that this region of the pore does influence the properties of channel gating (9,16). However, the importance of this region seems to be in determining the mean open time of the channel, and mutations in each subunit appear to act independently as if these residues do not form a direct constriction that could form a gate (7,17).
Molecular mechanisms and binding site locations for noncompetitive antagonists of nicotinic acetylcholine receptors
2006, International Journal of Biochemistry and Cell Biology