Identification and functional characterization of a novel acetylcholine-binding protein from the marine annelid Capitella teleta.

Biochemistry
Thomas McCormackJerrel L Yakel

Abstract

We identified a homologue of the molluscan acetylcholine-binding protein (AChBP) in the marine polychaete Capitella teleta, from the annelid phylum. The amino acid sequence of C. teleta AChBP (ct-AChBP) is 21-30% identical with those of known molluscan AChBPs. Sequence alignments indicate that ct-AChBP has a shortened Cys loop compared to other Cys loop receptors, and a variation on a conserved Cys loop triad, which is associated with ligand binding in other AChBPs and nicotinic ACh receptor (nAChR) alpha subunits. Within the D loop of ct-AChBP, a conserved aromatic residue (Tyr or Trp) in nAChRs and molluscan AChBPs, which has been implicated directly in ligand binding, is substituted with an isoleucine. Mass spectrometry results indicate that Asn122 and Asn216 of ct-AChBP are glycosylated when expressed using HEK293 cells. Small-angle X-ray scattering data suggest that the overall shape of ct-AChBP in the apo or unliganded state is similar to that of homologues with known pentameric crystal structures. NMR experiments show that acetylcholine, nicotine, and alpha-bungarotoxin bind to ct-AChBP with high affinity, with K(D) values of 28.7 microM, 209 nM, and 110 nM, respectively. Choline bound with a lower affinity (K(D) = 163 m...Continue Reading

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Citations

Jan 12, 2013·Pflügers Archiv : European journal of physiology·Jerrel L Yakel
Jul 16, 2013·Biochemical Pharmacology·Mieke NysChris Ulens
May 24, 2012·Proceedings of the National Academy of Sciences of the United States of America·Bert BillenChris Ulens
May 1, 2020·Neuropharmacology·Gisela Andrea Camacho-Hernandez, Palmer Taylor
Apr 12, 2014·Chemical Reviews·Kalyana B AkondiPaul F Alewood
Jun 6, 2014·Journal of Medicinal Chemistry·Li-Fang YuAlan P Kozikowski

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