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Identification of binding domains in the sodium channel Na V 1.8 intracellular N‐terminal region and annexin II light chain p11
Author(s) -
Poon W.-Y.Louisa,
Malik-Hall Misbah,
Wood John N.,
Okuse Kenji
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01512-6
Subject(s) - sodium channel , chemistry , gene isoform , sodium , binding site , immunoglobulin light chain , stereochemistry , biophysics , microbiology and biotechnology , biochemistry , biology , gene , organic chemistry , antibody , immunology
The interaction of p11 (annexin II light chain) with the N‐terminal domain of Na V 1.8, a tetrodotoxin‐resistant sodium channel, is essential for the functional expression of the channel. Here we show that p11 binds to Na V 1.8 but not to sodium channel isoforms Na V 1.2, 1.5, 1.7 or Na V 1.9. The binding of amino acids 74–103 of Na V 1.8 to p11 residues 33–78 occurs in a random coiled region flanked by two EF hand motifs whose crystal structure has been established. As Na V 1.8 channel expression is associated with pain pathways, drugs that disrupt the Na V 1.8–p11 interaction and down‐regulate channel expression may have analgesic activity.