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Studies on sea snake venom

Erabutoxins a and b are neurotoxins isolated from venom of a sea snake Laticauda semifasciata (erabu-umihebi). Amino acid sequences of the toxins indicated that the toxins are members of a superfamily consisting of short and long neurotoxins and cytotoxins found in sea snakes and terrestrial snakes....

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Detalles Bibliográficos
Autores principales: TAMIYA, Nobuo, YAGI, Tatsuhiko
Formato: Texto
Lenguaje:English
Publicado: The Japan Academy 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3066545/
https://www.ncbi.nlm.nih.gov/pubmed/21422738
http://dx.doi.org/10.2183/pjab.87.41
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author TAMIYA, Nobuo
YAGI, Tatsuhiko
author_facet TAMIYA, Nobuo
YAGI, Tatsuhiko
author_sort TAMIYA, Nobuo
collection PubMed
description Erabutoxins a and b are neurotoxins isolated from venom of a sea snake Laticauda semifasciata (erabu-umihebi). Amino acid sequences of the toxins indicated that the toxins are members of a superfamily consisting of short and long neurotoxins and cytotoxins found in sea snakes and terrestrial snakes. The short neurotoxins to which erabutoxins belong act by blocking the nicotinic acetylcholine receptor on the post synaptic membrane in a manner similar to that of curare. X-ray crystallography and NMR analyses showed that the toxins have a three-finger structure, in which three fingers made of three loops emerging from a dense core make a gently concave surface of the protein. The sequence comparison and the location of essential residues on the protein suggested the mechanism of binding of the toxin to the acetylcholine receptor. Classification of snakes by means of sequence comparison and that based on different morphological features were inconsistent, which led the authors to propose a hypothesis “Evolution without divergence.”
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spelling pubmed-30665452011-05-19 Studies on sea snake venom TAMIYA, Nobuo YAGI, Tatsuhiko Proc Jpn Acad Ser B Phys Biol Sci Review Erabutoxins a and b are neurotoxins isolated from venom of a sea snake Laticauda semifasciata (erabu-umihebi). Amino acid sequences of the toxins indicated that the toxins are members of a superfamily consisting of short and long neurotoxins and cytotoxins found in sea snakes and terrestrial snakes. The short neurotoxins to which erabutoxins belong act by blocking the nicotinic acetylcholine receptor on the post synaptic membrane in a manner similar to that of curare. X-ray crystallography and NMR analyses showed that the toxins have a three-finger structure, in which three fingers made of three loops emerging from a dense core make a gently concave surface of the protein. The sequence comparison and the location of essential residues on the protein suggested the mechanism of binding of the toxin to the acetylcholine receptor. Classification of snakes by means of sequence comparison and that based on different morphological features were inconsistent, which led the authors to propose a hypothesis “Evolution without divergence.” The Japan Academy 2011-03-11 /pmc/articles/PMC3066545/ /pubmed/21422738 http://dx.doi.org/10.2183/pjab.87.41 Text en © 2011 The Japan Academy This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review
TAMIYA, Nobuo
YAGI, Tatsuhiko
Studies on sea snake venom
title Studies on sea snake venom
title_full Studies on sea snake venom
title_fullStr Studies on sea snake venom
title_full_unstemmed Studies on sea snake venom
title_short Studies on sea snake venom
title_sort studies on sea snake venom
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3066545/
https://www.ncbi.nlm.nih.gov/pubmed/21422738
http://dx.doi.org/10.2183/pjab.87.41
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