Agonist-mediated Conformational Changes in Acetylcholine-binding Protein Revealed by Simulation and Intrinsic Tryptophan Fluorescence
Open Access
- 1 March 2005
- journal article
- Published by Elsevier BV in Journal of Biological Chemistry
- Vol. 280 (9), 8443-8451
- https://doi.org/10.1074/jbc.m412389200
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Coupling of agonist binding to channel gating in an ACh-binding protein linked to an ion channelNature, 2004
- Nicotine and Carbamylcholine Binding to Nicotinic Acetylcholine Receptors as Studied in AChBP Crystal StructuresNeuron, 2004
- Curariform Antagonists Bind in Different Orientations to the Nicotinic Receptor Ligand Binding DomainPublished by Elsevier BV ,2003
- Curariform Antagonists Bind in Different Orientations to Acetylcholine-binding ProteinJournal of Biological Chemistry, 2003
- The nicotinic receptor ligand binding domainJournal of Neurobiology, 2002
- Tryptophan Fluorescence Reveals Conformational Changes in the Acetylcholine Binding ProteinPublished by Elsevier BV ,2002
- Lysine Scanning Mutagenesis Delineates Structural Model of the Nicotinic Receptor Ligand Binding DomainJournal of Biological Chemistry, 2002
- Residues in the ε Subunit of the Nicotinic Acetylcholine Receptor Interact To Confer Selectivity of Waglerin-1 for the α−ε Subunit Interface SiteBiochemistry, 2002
- AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of moleculesComputer Physics Communications, 1995
- Electron transfers in chemistry and biologyBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1985