Key result
ApoCaM bound to the NaV1.1 IQ domain preferentially more than Ca2+/CaM, with the C-lobe predominant for apoCaM binding and the N-lobe predominant for Ca2+/CaM binding.
This study elucidates the molecular mechanisms by which Ca2+, lobe-specificity, and CaMKII modulate Calmodulin binding to the NaV1.1 voltage-gated sodium channel.
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May modulate NaV1.1 gating in excitable cells; leaves open relevance to human channelopathies.
Li et al. (2018) studied this question. Ca2+, lobe-specificity, and CaMKII was evaluated on Binding of CaM to NaV1.1 IQ domain. ApoCaM bound to the NaV1.1 IQ domain preferentially more than Ca2+/CaM, with the C-lobe predominant for apoCaM binding and the N-lobe predominant for Ca2+/CaM binding.
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