2PDZ

SOLUTION STRUCTURE OF THE SYNTROPHIN PDZ DOMAIN IN COMPLEX WITH THE PEPTIDE GVKESLV, NMR, 15 STRUCTURES

Summary for 2PDZ

• Entry DOI: 10.2210/pdb2pdz/pdb
• Descriptor: SYNTROPHIN, PEPTIDE GVKESLV (2 entities in total)
• Functional Keywords: syntrophin pdz domain, voltage-gated sodium channel, complex (syntrophin-peptide), complex (syntrophin-peptide) complex, complex (syntrophin/peptide)
• Biological source: Mus musculus (house mouse)
• Cellular location: Cell membrane, sarcolemma; Peripheral membrane protein; Cytoplasmic side: Q61234
• Total number of polymer chains: 2
• Total formula weight: 9831.44

Authors

Schultz, J.,Hoffmueller, U.,Ashurst, J.,Krause, G.,Schmieder, P.,Macias, M.,Schneider-Mergener, J.,Oschkinat, H. (deposition date: 1997-12-10, release date: 1998-12-30, Last modification date: 2024-05-22)

Primary citation

Schultz, J.,Hoffmuller, U.,Krause, G.,Ashurst, J.,Macias, M.J.,Schmieder, P.,Schneider-Mergener, J.,Oschkinat, H.
Specific interactions between the syntrophin PDZ domain and voltage-gated sodium channels.
Nat.Struct.Biol., 5:19-24, 1998

PubMed 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 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.

PubMed: 9437424
DOI: 10.1038/nsb0198-19

Experimental method

SOLUTION NMR