Interactions between α-conotoxin MI and the Torpedo marmorata receptor α–δ interface
The muscle-type nicotinic receptor has two distinguishable acetylcholine binding sites at the α–γ and α–δ subunit interfaces; α-conotoxins can bind them selectively. Moreover, we previously reported that α-conotoxin MI can interact with Torpedo californica and Torpedo marmorata receptors showing tha...
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Veröffentlicht in: | Biochemical and biophysical research communications 2007-03, Vol.355 (1), p.275-279 |
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Sprache: | eng |
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Zusammenfassung: | The muscle-type nicotinic receptor has two distinguishable acetylcholine binding sites at the α–γ and α–δ subunit interfaces; α-conotoxins can bind them selectively. Moreover, we previously reported that α-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 Jiménez 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 α-conotoxin MI binding, a photoactivatable reagent was used and labeled sites were mapped by enzymatic proteolysis, MALDI-TOF-MS and Edman degradation. α-Conotoxin MI binding determinants were found and studies revealed a second binding motif at the α/δ interface. A proposal for receptor–toxin interaction is discussed based on experimental results and docking studies. |
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ISSN: | 0006-291X 1090-2104 1090-2104 |
DOI: | 10.1016/j.bbrc.2007.01.154 |