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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

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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

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

  1. SDG 14 - Life Below Water
    SDG 14 Life Below Water

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