1I9B

X-RAY STRUCTURE OF ACETYLCHOLINE BINDING PROTEIN (ACHBP)

Summary for 1I9B

• Entry DOI: 10.2210/pdb1i9b/pdb
• Descriptor: ACETYLCHOLINE BINDING PROTEIN, CALCIUM ION, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (4 entities in total)
• Functional Keywords: pentamer, igg fold, ligand binding protein
• Biological source: Lymnaea stagnalis (great pond snail)
• Cellular location: Secreted: P58154
• Total number of polymer chains: 5
• Total formula weight: 124953.86

Authors

Brejc, K.,van Dijk, W.J.,Klaassen, R.,Schuurmans, M.,van der Oost, J.,Smit, A.B.,Sixma, T.K. (deposition date: 2001-03-18, release date: 2001-05-16, Last modification date: 2018-03-07)

Primary citation

Brejc, K.,van Dijk, W.J.,Klaassen, R.V.,Schuurmans, M.,van Der Oost, J.,Smit, A.B.,Sixma, T.K.
Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors.
Nature, 411:269-276, 2001

PubMed Abstract: Pentameric ligand gated ion-channels, or Cys-loop receptors, mediate rapid chemical transmission of signals. This superfamily of allosteric transmembrane proteins includes the nicotinic acetylcholine (nAChR), serotonin 5-HT3, gamma-aminobutyric-acid (GABAA and GABAC) and glycine receptors. Biochemical and electrophysiological information on the prototypic nAChRs is abundant but structural data at atomic resolution have been missing. Here we present the crystal structure of molluscan acetylcholine-binding protein (AChBP), a structural and functional homologue of the amino-terminal ligand-binding domain of an nAChR alpha-subunit. In the AChBP homopentamer, the protomers have an immunoglobulin-like topology. Ligand-binding sites are located at each of five subunit interfaces and contain residues contributed by biochemically determined 'loops' A to F. The subunit interfaces are highly variable within the ion-channel family, whereas the conserved residues stabilize the protomer fold. This AChBP structure is relevant for the development of drugs against, for example, Alzheimer's disease and nicotine addiction.

PubMed: 11357122
DOI: 10.1038/35077011

Experimental method

X-RAY DIFFRACTION (2.7 Å)