Principal pathway coupling agonist binding to channel gating in nicotinic receptors (Q46799020)

25 December 2017

title

Principal pathway coupling agonist binding to channel gating in nicotinic receptors (English)

1 reference

25 December 2017

author name string

Won Yong Lee

series ordinal

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25 December 2017

Steven M Sine

series ordinal

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25 December 2017

language of work or name

English

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publication date

1 November 2005

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25 December 2017

published in

Nature

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25 December 2017

volume

438

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25 December 2017

issue

7065

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25 December 2017

page(s)

243-247

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25 December 2017

Refined structure of the nicotinic acetylcholine receptor at 4A resolution

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Activation of the nicotinic acetylcholine receptor involves a switch in conformation of the alpha subunits.

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Activation of Torpedo acetylcholine receptors expressed in mouse fibroblasts. Single channel current kinetics reveal distinct agonist binding affinities

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Mapping the conformational wave of acetylcholine receptor channel gating

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Invariant aspartic Acid in muscle nicotinic receptor contributes selectively to the kinetics of agonist binding

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A novel hyperekplexia-causing mutation in the pre-transmembrane segment 1 of the human glycine receptor alpha1 subunit reduces membrane expression and impairs gating by agonists.

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Multiple roles of the conserved key residue arginine 209 in neuronal nicotinic receptors.

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Charged Residues in the β2 Subunit Involved in GABAA Receptor Activation

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Arginine 222 in the pre-transmembrane domain 1 of 5-HT3A receptors links agonist binding to channel gating

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The location of the gate in the acetylcholine receptor channel

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A highly conserved aspartic acid residue in the signature disulfide loop of the alpha 1 subunit is a determinant of gating in the glycine receptor

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Role of charged residues in coupling ligand binding and channel activation in the extracellular domain of the glycine receptor.

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Naturally occurring mutations at the acetylcholine receptor binding site independently alter ACh binding and channel gating.

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Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins

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inferred from DOI database lookup

7 January 2021

based on heuristic

A structural double-mutant cycle: estimating the strength of a buried salt bridge in barnase

1 reference

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1038/NATURE04156

1 reference

25 December 2017

Dimensions Publication ID

1051471722

0 references

1 reference

25 December 2017