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Specific interactions between the syntrophin PDZ domain and voltage-gated sodium channels

Nature Structural Biology volume 5, pages 19–24 (1998)Cite this article

Abstract

Syntrophins are modular proteins belonging to the dystrophin associated glycoprotein complex and are thought to be involved in the regulation of the muscular system. Screening of peptide libraries revealed selectivity of the synotrophin PDZ domain toward the motif R/K/Q-E-S/T-X-V-COO− found to be highly conserved in the α-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.

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Author notes

  1. Jennifer Ashurst

    Present address: Dept. of Plant Sciences, University of Cambridge, Downing St., Cambridge, CB2 3EA, Great Britain

Authors and Affiliations

  1. Forschungsinstitut für Molekulare Pharmakologie, Alfred-Kowalke-Straβe 4, 10315, Berlin, Germany

    Johan Schultz, Gerd Krause, Maria J. Macias, Peter Schmieder & Hartmut Oschkinat

  2. Institut für Medizinische Immunologie, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Schumannstr. 20-21, 10098, Berlin, Germany

    Ulrich Hoffmuüller & Jens Schneider-Mergener

  3. European Molecular Biology Laboratory, Meyerhofstraβe 1, 69012, Heidelberg, Germany

    Jennifer Ashurst & Maria J. Macias

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  1. Johan Schultz
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Correspondence to Maria J. Macias or Hartmut Oschkinat.

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Schultz, J., Hoffmuüller, U., Krause, G. et al. Specific interactions between the syntrophin PDZ domain and voltage-gated sodium channels. Nat Struct Mol Biol 5, 19–24 (1998). https://doi.org/10.1038/nsb0198-19

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