Johan Schultz1, Ulrich Hoffmuüller2, Gerd Krause1, Jennifer Ashurst3, 4, Maria J. Macias1, 3, 6, Peter Schmieder1, Jens Schneider-Mergener2
& Hartmut Oschkinat1, 5
1Forschungsinstitut für Molekulare Pharmakologie, Alfred-Kowalke-Stra
e 4, 10315 Berlin, Germany.
2Institut für Medizinische Immunologie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Schumannstr. 20-21, 10098 Berlin, Germany.
3European Molecular Biology Laboratory, Meyerhofstrae 1, 69012 Heidelberg, Germany.
4Present address: Dept. of Plant Sciences, University of Cambridge, Downing St., Cambridge CB2 3EA, Great Britain.
5email: Oschkinat@fmp-berlin.de
6email: Marcias@embl-heidelberg.de
-subunit C-terminus of vertebrate voltage gated sodium channels (VGSCs). The solution structure of the domain in complex with the peptide G-V-K-E-S-L-V shows specific interactions between the conserved residues in the peptide and syntrophin-characteristic residues of the domain. We propose that syntrophins localize VGSCs to the dystrophin network through its PDZ domain.
