Structural determinants of selective alpha-conotoxin binding to a nicotinic acetylcholine receptor homolog AChBP

C. Ulens, R.C. Hogg, P.H. Celie, D. Bertrand, V. Tsetlin, A.B. Smit, T.K. Sixma

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

The nicotinic acetylcholine receptor (nAChR) is the prototype member of the super-family of pentameric ligand-gated ion channels. How the extracellular ligand-binding domain coordinates selective binding of ligand molecules to different subtypes of the receptor is unknown at the structural level. Here, we present the 2.2-Å crystal structure of a homolog of the ligand-binding domain of the nAChR, Aplysia californica AChBP (Ac-AChBP), in complex with α-conotoxin ImI. This conotoxin is unique in its selectivity toward the neuronal α
Original languageEnglish
Pages (from-to)3615-3620
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume103
DOIs
Publication statusPublished - 2006

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