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These conditions do not distinguish the CaM binding mode and indeed, they could support both cis- and trans-CaM binding.
Here, we investigated the contribution of helix D to CaM binding.
Accordingly, the relationship between the coiled-coil and CaM binding domains has been examined recently in Kv7.2 channels, suggesting that the stability of the helix D coiled-coil affects CaM binding and that it results in altered PIP2 sensitivity32.
We present evidence supporting the notion that the coiled-coil formed by helix D distal to the AB CaM-binding module indirectly favors trans-binding of CaM to Kv7.2, and that CaM binding stabilizes the tetrameric C-terminal assembly.
Thus, the presence of a tetrameric coiled-coil following the CaM binding site stabilizes the AB/CaM complex.
We used the computational protein design approach to modify CaM binding specificity for these two targets.
Similar(17)
How this interaction affects the propensity to adopt the trans- or cis-CaM binding is still not known.
Accordingly, the presence of both peptides eliminated Ca2+-CaM binding to the NR1 subunits (Fig. 2).
Thus, our data reveal an important reciprocal crosstalk between CaM-binding and the subunit-recognition domains of Kv7 channels.
Illustrative of the versatility of CaM, over 50 CaM-binding proteins are also described.
There are seven TRPCs, all of which have a Ca(2+ -dependent calmodulin (CaM)-binding domain in their C termini.
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