Structural basis for recognition of synaptic vesicle protein 2C by botulinum neurotoxin A

Roger M. Benoit, Daniel Frey, Manuel Hilbert, Josta T. Kevenaar, Mara M. Wieser, Christian U. Stirnimann, David McMillan, Tom Ceska, Florence Lebon, Rolf Jaussi, Michel O. Steinmetz, Gebhard F. X. Schertler, Casper C. Hoogenraad, Guido Capitani and Richard A. Kammerer ()
Additional contact information
Roger M. Benoit: Laboratory of Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland
Daniel Frey: Laboratory of Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland
Manuel Hilbert: Laboratory of Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland
Josta T. Kevenaar: Cell Biology, Faculty of Science, Utrecht University, 3584 CH Utrecht, The Netherlands
Mara M. Wieser: Laboratory of Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland
Christian U. Stirnimann: Swiss Light Source, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland
David McMillan: UCB Celltech, UCB Pharma, UCB NewMedicines, Slough SL1 4EN, UK
Tom Ceska: UCB Celltech, UCB Pharma, UCB NewMedicines, Slough SL1 4EN, UK
Florence Lebon: UCB Pharma, UCB NewMedicines, B-1420 Braine-L’Alleud, Belgium
Rolf Jaussi: Laboratory of Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland
Michel O. Steinmetz: Laboratory of Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland
Gebhard F. X. Schertler: Laboratory of Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland
Casper C. Hoogenraad: Cell Biology, Faculty of Science, Utrecht University, 3584 CH Utrecht, The Netherlands
Guido Capitani: Laboratory of Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland
Richard A. Kammerer: Laboratory of Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland

Nature, 2014, vol. 505, issue 7481, 108-111

Abstract: Botulinum neurotoxin A (BoNT/A) is considered the most toxic substance known but is also used as a therapeutic drug for a growing number of diseases and conditions; researchers have now obtained a high-resolution crystal structure of the receptor-binding domain of the BoNT/A in complex with the luminal domain of synaptic vesicle protein 2C (SV2C), one of its receptors, allowing the identification of a peptide that can inhibit complex formation.

Date: 2014
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DOI: 10.1038/nature12732

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