caa a22 4500 477137857 CHVBK 20180405111724.0 cr unu---uuuuu 170330e19971201xx s 000 0 eng 10.1007/BF02442877 doi (NATIONALLICENCE)springer-10.1007/BF02442877 Allosteric-type control of synaptobrevin cleavage by tetanus toxin light chain [Elektronische Daten] [Fabrice Cornille, Loïc Martin, Christine Lenoir, Didier Cussac, Bernard Roques, Marie-Claude Fournié-Zaluski] Summary: The light chain of tetanus neurotoxin (TeNTL chain) has been shown to be endowed with zine endopeptidase activity, selectively directed towards the Gln76-Phe77 bond of synaptobrevin, a vesicle-associated membrane protein critically involved in neuroexocytosis. In previous reports, truncations at the NH2- and COOH-terminus of synaptobrevin have shown that the sequence 39-88 of synaptobrevin is the minimum substrate of TeNT, suggesting either the requirement of a well-defined three-dimensional structure of synaptobrevin or a role in the mechanism of substrate hydrolysis for residues distal from the cleavage site. In this study, the addition of NH2- and COOH-terminal peptides of synaptobrevin, S 27-55 (S1) and S 82-93 (S2), to the synaptobrevin fragment S 56-81 allowed the cleavage of this latter peptide by TeNT to occur. This appears to result from an activation process mediated by the simultaneous binding of S1 and S2 with complementary sites present on TeNT as shown by surface plasmon resonance experiments. All these results favor an exosite-controlled hydrolysis of synaptobrevin by TeNT probably involving a conformational change of the toxin. This could accound for the high degree of substrate specificity of TeNT and, probably, botulinum neurotoxins. Kluwer Academic Publishers, 1997 Zinc endopeptidase nationallicence Clostridial neurotoxins nationallicence Cornille Fabrice Départment de Pharmacochimie Moléculaire et Structurale, U266 INSERM, URA D1500 CNRS, Université René Descartes, UFR des Sciences Pharmaceutiques et Biologiques, 4 Avenue de l'Observatoire, F-75270, Paris Cedex 06, France aut Martin Loïc Départment de Pharmacochimie Moléculaire et Structurale, U266 INSERM, URA D1500 CNRS, Université René Descartes, UFR des Sciences Pharmaceutiques et Biologiques, 4 Avenue de l'Observatoire, F-75270, Paris Cedex 06, France aut Lenoir Christine Départment de Pharmacochimie Moléculaire et Structurale, U266 INSERM, URA D1500 CNRS, Université René Descartes, UFR des Sciences Pharmaceutiques et Biologiques, 4 Avenue de l'Observatoire, F-75270, Paris Cedex 06, France aut Cussac Didier Départment de Pharmacochimie Moléculaire et Structurale, U266 INSERM, URA D1500 CNRS, Université René Descartes, UFR des Sciences Pharmaceutiques et Biologiques, 4 Avenue de l'Observatoire, F-75270, Paris Cedex 06, France aut Roques Bernard Départment de Pharmacochimie Moléculaire et Structurale, U266 INSERM, URA D1500 CNRS, Université René Descartes, UFR des Sciences Pharmaceutiques et Biologiques, 4 Avenue de l'Observatoire, F-75270, Paris Cedex 06, France aut Fournié-Zaluski Marie-Claude Départment de Pharmacochimie Moléculaire et Structurale, U266 INSERM, URA D1500 CNRS, Université René Descartes, UFR des Sciences Pharmaceutiques et Biologiques, 4 Avenue de l'Observatoire, F-75270, Paris Cedex 06, France aut Letters in Peptide Science Kluwer Academic Publishers 4/4-6(1997-12-01), 207-212 0929-5666 4:4-6<207 1997 4 10989 https://doi.org/10.1007/BF02442877 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF02442877 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Cornille Fabrice Départment de Pharmacochimie Moléculaire et Structurale, U266 INSERM, URA D1500 CNRS, Université René Descartes, UFR des Sciences Pharmaceutiques et Biologiques, 4 Avenue de l'Observatoire, F-75270, Paris Cedex 06, France aut NATIONALLICENCE 700 1- Martin Loïc Départment de Pharmacochimie Moléculaire et Structurale, U266 INSERM, URA D1500 CNRS, Université René Descartes, UFR des Sciences Pharmaceutiques et Biologiques, 4 Avenue de l'Observatoire, F-75270, Paris Cedex 06, France aut NATIONALLICENCE 700 1- Lenoir Christine Départment de Pharmacochimie Moléculaire et Structurale, U266 INSERM, URA D1500 CNRS, Université René Descartes, UFR des Sciences Pharmaceutiques et Biologiques, 4 Avenue de l'Observatoire, F-75270, Paris Cedex 06, France aut NATIONALLICENCE 700 1- Cussac Didier Départment de Pharmacochimie Moléculaire et Structurale, U266 INSERM, URA D1500 CNRS, Université René Descartes, UFR des Sciences Pharmaceutiques et Biologiques, 4 Avenue de l'Observatoire, F-75270, Paris Cedex 06, France aut NATIONALLICENCE 700 1- Roques Bernard Départment de Pharmacochimie Moléculaire et Structurale, U266 INSERM, URA D1500 CNRS, Université René Descartes, UFR des Sciences Pharmaceutiques et Biologiques, 4 Avenue de l'Observatoire, F-75270, Paris Cedex 06, France aut NATIONALLICENCE 700 1- Fournié-Zaluski Marie-Claude Départment de Pharmacochimie Moléculaire et Structurale, U266 INSERM, URA D1500 CNRS, Université René Descartes, UFR des Sciences Pharmaceutiques et Biologiques, 4 Avenue de l'Observatoire, F-75270, Paris Cedex 06, France aut NATIONALLICENCE 773 0- Letters in Peptide Science Kluwer Academic Publishers 4/4-6(1997-12-01), 207-212 0929-5666 4:4-6<207 1997 4 10989 Metadata rights reserved Springer special CC-BY-NC licence nationallicence SWISSBIB 477137857 BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer