Download full-text PDF |
Source |
|---|
Publication Analysis
Top Keywords
Similar Publications
Curariform antagonists bind in different orientations to acetylcholine-binding protein.
J Biol Chem
June 2003
Receptor Biology Laboratory, Department of Physiology and Biophysics, Mayo Clinic Department of Pharmacology, Mayo Graduate School, Rochester, Minnesota 55905, USA.
Acetylcholine-binding protein (AChBP) recently emerged as a prototype for relating structure to function of the ligand binding domain of nicotinic acetylcholine receptors (AChRs). To understand interactions of competitive antagonists at the atomic structural level, we studied binding of the curare derivatives d-tubocurarine (d-TC) and metocurine to AChBP using computational methods, mutagenesis, and ligand binding measurements. To account for protein flexibility, we used a 2-ns molecular dynamics simulation of AChBP to generate multiple snapshots of the equilibrated dynamic structure to which optimal docking orientations were determined.
View Article and Find Full Text PDFThe alpha-conotoxins GI and MI distinguish between the nicotinic acetylcholine receptor agonist sites while SI does not.
Biochemistry
November 1994
Department of Biochemistry, Universidad Central del Caribe, Bayamón, Puerto Rico 00960.
The alpha-conotoxins are paralytic peptide toxins from Indo-Pacific cone snails. This paper presents a detailed analysis of how alpha-conotoxins inhibit [125I]-alpha-bungarotoxin (125I-BTX) equilibrium binding to the acetylcholine receptor (AChR) from electric organ of Torpedo californica and Torpedo nobiliana. All three alpha-conotoxins studied, SI, GI, and MI, completely inhibited 125I-BTX binding with the same order of potency in both species (MI approximately GI > SI approximately d-tubocurarine).
View Article and Find Full Text PDFMolecular dissection of subunit interfaces in the acetylcholine receptor: identification of residues that determine curare selectivity.
Proc Natl Acad Sci U S A
October 1993
Department of Physiology and Biophysics, Mayo Clinic, Rochester, MN 55905.
The acetylcholine receptor from vertebrate skeletal muscle is a transmembrane channel that binds nerve-released acetylcholine to elicit rapid transport of small cations. Composed of two alpha subunits and one beta, one gamma, and one delta subunit, the receptor is a cooperative protein containing two sites that bind agonists, curariform antagonists, and snake alpha-toxins. Until recently the two binding sites were thought to reside entirely within each of the two alpha subunits, but affinity labeling and expression studies have demonstrated contributions by the gamma and delta subunits.
View Article and Find Full Text PDF[Role of vecuronium in comparison with curariform drugs used in man].
Ann Fr Anesth Reanim
November 1983
Vecuronium, a new non-depolarizing muscle relaxant, was more powerful than d-tubocurarine, gallamine and alcuronium. Its muscle blocking effect was similar to that of pancuronium. It had a smaller distribution volume and a quicker elimination half-life than the other non-depolarizing muscle blocking drugs.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!