Interactions between alpha-conotoxin MI and the Torpedo marmorata receptor alpha-delta interface
2007 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 355, no 1, 275-279 p.Article in journal (Refereed) Published
The muscle-type nicotinic receptor has two distinguishable acetylcholine binding sites at the alpha-gamma and alpha-delta subunit interfaces; alpha-conotoxins can bind them selectively. Moreover, we previously reported that alpha-conotoxin MI can interact with Torpedo californica and Torpedo marmorata receptors showing that conotoxins can also detect receptors from different species of the same genus [L. Cortez, S.G. del Canto, F. Testai, M.B. de Jimenez Bonino, Conotoxin MI inhibits the acetylcholine binding site of the Torpedo marmorata receptor, Biochem. Biophys. Res. Commun. 295 (2002) 791-795]. Herein, to identify T. marmorata receptor regions involved in alpha-conotoxin MI binding, a photoactivatable reagent was used and labeled sites were mapped by enzymatic proteolysis, MALDI-TOF-MS and Edman degradation. alpha-Conotoxin MI binding determinants were found and studies revealed a second binding motif at the alpha/delta interface. A proposal for receptor-toxin interaction is discussed based on experimental results and docking studies.
Place, publisher, year, edition, pages
2007. Vol. 355, no 1, 275-279 p.
α-Conotoxin MI, Conus, Ligand-binding sites, Nicotinic receptors, Torpedo marmorata
Medical and Health Sciences
IdentifiersURN: urn:nbn:se:uu:diva-10287DOI: 10.1016/j.bbrc.2007.01.154ISI: 000244641200046PubMedID: 17292857OAI: oai:DiVA.org:uu-10287DiVA: diva2:38055