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Specific interactions between the syntrophin PDZ domain and voltage-gated sodium channels.
Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany.
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 alpha-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 in the domain. We propose that syntrophins localize VGSCs to the dystrophin network through its PDZ domain.
PMID: 9437424 [PubMed - indexed for MEDLINE]
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Cited by 14 PubMed Central articles
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Predicting PDZ domain-peptide interactions from primary sequences.
Chen JR, Chang BH, Allen JE, Stiffler MA, MacBeath G.
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[Nat Biotechnol. 2008]
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Anchoring TRP to the INAD macromolecular complex requires the last 14 residues in its carboxyl terminus.
Peng L, Popescu DC, Wang N, Shieh BH.
J Neurochem. 2008 Mar; 104(6):1526-35. Epub 2007 Nov 22.
[J Neurochem. 2008]
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{alpha}-Syntrophin regulates ARMS localization at the neuromuscular junction and enhances EphA4 signaling in an ARMS-dependent manner.
Luo S, Chen Y, Lai KO, Arévalo JC, Froehner SC, Adams ME, Chao MV, Ip NY.
J Cell Biol. 2005 Jun 6; 169(5):813-24.
[J Cell Biol. 2005]
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Structures reported by this article