[HTML][HTML] Identification of binding domains in the sodium channel NaV1. 8 intracellular N-terminal region and annexin II light chain p11
WYL Poon, M Malik-Hall, JN Wood, K Okuse - FEBS letters, 2004 - Elsevier
WYL Poon, M Malik-Hall, JN Wood, K Okuse
FEBS letters, 2004•ElsevierThe interaction of p11 (annexin II light chain) with the N-terminal domain of NaV1. 8, a
tetrodotoxin-resistant sodium channel, is essential for the functional expression of the
channel. Here we show that p11 binds to NaV1. 8 but not to sodium channel isoforms NaV1.
2, 1.5, 1.7 or NaV1. 9. The binding of amino acids 74–103 of NaV1. 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 NaV1. 8 channel expression is associated with pain pathways, drugs …
tetrodotoxin-resistant sodium channel, is essential for the functional expression of the
channel. Here we show that p11 binds to NaV1. 8 but not to sodium channel isoforms NaV1.
2, 1.5, 1.7 or NaV1. 9. The binding of amino acids 74–103 of NaV1. 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 NaV1. 8 channel expression is associated with pain pathways, drugs …
The interaction of p11 (annexin II light chain) with the N-terminal domain of NaV1.8, a tetrodotoxin-resistant sodium channel, is essential for the functional expression of the channel. Here we show that p11 binds to NaV1.8 but not to sodium channel isoforms NaV1.2, 1.5, 1.7 or NaV1.9. The binding of amino acids 74–103 of NaV1.8 to p11 residues 33–78 occurs in a random coiled region flanked by two EF hand motifs whose crystal structure has been established. As NaV1.8 channel expression is associated with pain pathways, drugs that disrupt the NaV1.8–p11 interaction and down-regulate channel expression may have analgesic activity.
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