scholarly journals Understanding structure-function relationships of the human neuronal acetylcholine receptor: insights from the first crystal structures of neuronal subunits

2017 ◽  
Vol 175 (11) ◽  
pp. 1880-1891 ◽  
Author(s):  
Petros Giastas ◽  
Marios Zouridakis ◽  
Socrates J Tzartos
Keyword(s):  
Structure Function ◽  
Crystal Structures ◽  
Acetylcholine Receptor ◽  
Neuronal Acetylcholine Receptor

scholarly journals Crystal structures of murine angiogenin‐2 and ‐3 – probing ‘structure – function’ relationships amongst angiogenin homologues

FEBS Journal ◽  
2012 ◽  
Vol 280 (1) ◽  
pp. 302-318 ◽  
Author(s):  
Shalini Iyer ◽  
Daniel E. Holloway ◽  
K. Ravi Acharya
Keyword(s):  
Structure Function ◽  
Crystal Structures

Expression of mRNAs in human thymus coding for the α3 subunit of a neuronal acetylcholine receptor

1991 ◽  
Vol 111 (2) ◽  
pp. 175-180 ◽  
Author(s):  
Mirta Mihovilovic ◽  
Allen D. Roses
Keyword(s):  
Acetylcholine Receptor ◽  
Human Thymus ◽  
Α3 Subunit ◽  
Neuronal Acetylcholine Receptor

Species-dependent metabolism of a novel selective α7 neuronal acetylcholine receptor agonist ABT-107

Xenobiotica ◽  
2013 ◽  
Vol 43 (9) ◽  
pp. 803-816 ◽  
Author(s):  
Hong Liu ◽  
Xiaoqing Deng ◽  
Jinrong Liu ◽  
Ning Liu ◽  
Patricia Stuart ◽  
...  
Keyword(s):  
Acetylcholine Receptor ◽  
Receptor Agonist ◽  
Neuronal Acetylcholine Receptor

Nicotinic Neuronal Acetylcholine Receptor ?-3 Subunit Transcription in Normal and Myasthenic Thymus

1993 ◽  
Vol 681 (1 Myasthenia Gr) ◽  
pp. 83-96 ◽  
Author(s):  
MIRTA MIHOVILOVIC ◽  
CHRISTINE HULETTE ◽  
JACQUELYN MITTELSTAEDT ◽  
CAROL AUSTIN ◽  
ALLEN D. ROSES
Keyword(s):  
Acetylcholine Receptor ◽  
Neuronal Acetylcholine Receptor

scholarly journals Rgg protein structure–function and inhibition by cyclic peptide compounds

2015 ◽  
Vol 112 (16) ◽  
pp. 5177-5182 ◽  
Author(s):  
Vijay Parashar ◽  
Chaitanya Aggarwal ◽  
Michael J. Federle ◽  
Matthew B. Neiditch
Keyword(s):  
Dna Binding ◽  
Structure Function ◽  
Cyclosporin A ◽  
Crystal Structures ◽  
Disulfide Bond ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
X Ray ◽  
Peptide Pheromone ◽  
Dimerization Interface

Peptide pheromone cell–cell signaling (quorum sensing) regulates the expression of diverse developmental phenotypes (including virulence) in Firmicutes, which includes common human pathogens, e.g.,Streptococcus pyogenesandStreptococcus pneumoniae. Cytoplasmic transcription factors known as “Rgg proteins” are peptide pheromone receptors ubiquitous in Firmicutes. Here we present X-ray crystal structures of aStreptococcusRgg protein alone and in complex with a tight-binding signaling antagonist, the cyclic undecapeptide cyclosporin A. To our knowledge, these represent the first Rgg protein X-ray crystal structures. Based on the results of extensive structure–function analysis, we reveal the peptide pheromone-binding site and the mechanism by which cyclosporin A inhibits activation of the peptide pheromone receptor. Guided by the Rgg–cyclosporin A complex structure, we predicted that the nonimmunosuppressive cyclosporin A analog valspodar would inhibit Rgg activation. Indeed, we found that, like cyclosporin A, valspodar inhibits peptide pheromone activation of conserved Rgg proteins in medically relevantStreptococcusspecies. Finally, the crystal structures presented here revealed that the Rgg protein DNA-binding domains are covalently linked across their dimerization interface by a disulfide bond formed by a highly conserved cysteine. The DNA-binding domain dimerization interface observed in our structures is essentially identical to the interfaces previously described for other members of the XRE DNA-binding domain family, but the presence of an intermolecular disulfide bond buried in this interface appears to be unique. We hypothesize that this disulfide bond may, under the right conditions, affect Rgg monomer–dimer equilibrium, stabilize Rgg conformation, or serve as a redox-sensitive switch.

scholarly journals A Dominant Mutation in a Neuronal Acetylcholine Receptor Subunit Leads to Motor Neuron Degeneration in Caenorhabditis elegans

2010 ◽  
Vol 30 (42) ◽  
pp. 13932-13942 ◽  
Author(s):  
B. Barbagallo ◽  
H. A. Prescott ◽  
P. Boyle ◽  
J. Climer ◽  
M. M. Francis
Keyword(s):  
Caenorhabditis Elegans ◽  
Motor Neuron ◽  
Acetylcholine Receptor ◽  
Receptor Subunit ◽  
Dominant Mutation ◽  
Motor Neuron Degeneration ◽  
Neuron Degeneration ◽  
Neuronal Acetylcholine Receptor

Acetylcholine Receptor Structure, Function, and Evolution

1985 ◽  
Vol 1 (1) ◽  
pp. 317-351 ◽  
Author(s):  
Robert M. Stroud ◽  
Janet Finer-Moore
Keyword(s):  
Structure Function ◽  
Acetylcholine Receptor ◽  
Receptor Structure
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