Structure and function of AChBP, homologue of the ligand‐binding domain of the nicotinic acetylcholine receptor

AB Smit, K BREJC, N Syed… - Annals of the New York …, 2003 - Wiley Online Library
Acetylcholine‐binding protein (AChBP) is a novel protein with high similarity to the
extracellular domain of the nicotinic acetylcholine receptor. AChBP lacks the …

The 2.7 Å Structure of AChBP, Homologue of the ligand‐binding domain of the nicotinic acetylcholine receptor

K Brejc, WJ van Dijk, AB Smit… - Ion Channels: From …, 2002 - Wiley Online Library
Acetylcholine binding protein (AChBP) is a novel protein with high similarity to the
extracellular domain of the nicotinic acetylcholine receptor. It is secreted from glia cells in the …

Acetylcholine-binding proteins: functional and structural homologs of nicotinic acetylcholine receptors.

AB Smit, PH Celie, IE Kasheverov… - Journal of molecular …, 2006 - europepmc.org
Acetylcholine-binding protein (AChBP) is a water-soluble protein released from molluscan
glial cells and modulates ACh-mediated synaptic transmission. Acetylcholine-binding …

Tryptophan fluorescence reveals conformational changes in the acetylcholine binding protein

SB Hansen, Z Radić, TT Talley, BE Molles… - Journal of Biological …, 2002 - ASBMB
The recent characterization of an acetylcholine binding protein (AChBP) from the fresh water
snail, Lymnaea stagnalis, shows it to be a structural homolog of the extracellular domain of …

The nicotinic receptor ligand binding domain

SM Sine - Journal of neurobiology, 2002 - Wiley Online Library
The ligand binding domain (LBD) of the nicotinic acetylcholine receptor has served as a
prototype for understanding molecular recognition in the family of neurotransmitter‐gated …

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

N Unwin, A Miyazawa, J Li, Y Fujiyoshi - Journal of molecular biology, 2002 - Elsevier
The nicotinic acetylcholine (ACh) receptor belongs to a superfamily of synaptic ion channels
that open in response to the binding of chemical transmitters. Their mechanism of activation …

[HTML][HTML] Assembly of mutant subunits of the nicotinic acetylcholine receptor lacking the conserved disulfide loop structure.

K Sumikawa, VM Gehle - Journal of Biological Chemistry, 1992 - Elsevier
Each subunit of the nicotinic acetylcholine receptor (AChR) contains two conserved cysteine
residues, which are known to form a disulfide bond, in the N-terminal extracellular domain …

Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins

A Karlin, MH Akabas - Neuron, 1995 - Elsevier
The nicotinic acetylcholine (ACh) receptors and the other neurotransmitter-gated ion
channels have key roles in fast synaptic transmission throughout the nervous system. These …

Galanthamine and non-competitive inhibitor binding to ACh-binding protein: evidence for a binding site on non-α-subunit interfaces of heteromeric neuronal nicotinic …

SB Hansen, P Taylor - Journal of molecular biology, 2007 - Elsevier
Rapid neurotransmission is mediated through a superfamily of Cys-loop receptors that
includes the nicotinic acetylcholine (nAChR), γ-aminobutyric acid (GABAA), serotonin (5 …

Structure of nicotinic acetylcholine receptors

A Karlin - Current opinion in neurobiology, 1993 - Elsevier
Nicotinic acetylcholine (ACh) receptors convert the binding of ACh into the opening of a
cation-conducting channel. New information about the regions of the receptor most …