Crystal structure of acetylcholine-binding protein from Bulinus truncatus reveals the conserved structural scaffold and sites of variation in nicotinic acetylcholine receptors

P.H.N. Celie, R.V. Klaassen, S.E. van Rossum-Fikkert, R. van Elk, P. van Nierop, A.B. Smit, T.K. Sixma

Research output: Contribution to JournalArticleAcademicpeer-review

88 Downloads (Pure)

Abstract

The crystal structure of acetylcholine-binding protein (AChBP) from the mollusk Lymnaea stagnalis is the established model for the ligand binding domains of the ligand-gated ion channel family, which includes nicotinic acetylcholine, 5-hydroxytryptamine (5-HT
Original languageEnglish
Pages (from-to)26457-26466
Number of pages10
JournalJournal of Biological Chemistry
Volume280
Issue number28
DOIs
Publication statusPublished - 2005

Fingerprint

Dive into the research topics of 'Crystal structure of acetylcholine-binding protein from Bulinus truncatus reveals the conserved structural scaffold and sites of variation in nicotinic acetylcholine receptors'. Together they form a unique fingerprint.

Cite this