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Na_V1.2 EFL domain allosterically enhances Ca²⁺ binding to sites I and II of WT and pathogenic calmodulin mutants bound to the channel CTD.

ABSTRACT: Neuronal voltage-gated sodium channel Na_V1.2 C-terminal domain (CTD) binds calmodulin (CaM) constitutively at its IQ motif. A solution structure (6BUT) and other NMR evidence showed that the CaM N domain (CaM_N) is structurally independent of the C-domain (CaM_C) whether CaM is bound to the Na_V1.2_IQp (1,901-1,927) or Na_V1.2_CTD (1,777-1,937) with or without calcium. However, in the CaM + Na_V1.2_CTD complex, the Ca²⁺ affinity of CaM_N was more favorable than in free CaM, while Ca²⁺ affinity for CaM_C was weaker than in the CaM + Na_V1.2_IQp complex. The CTD EF-like (EFL) domain allosterically widened the energetic gap between CaM domain

SUBMITTER: Mahling R

PROVIDER: S-EPMC8458505 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature

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Na_V1.2 EFL domain allosterically enhances Ca²⁺ binding to sites I and II of WT and pathogenic calmodulin mutants bound to the channel CTD.

OmicsDI is part of the ELIXIR infrastructure

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Dataset Information

NaV1.2 EFL domain allosterically enhances Ca2+ binding to sites I and II of WT and pathogenic calmodulin mutants bound to the channel CTD.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Na_V1.2 EFL domain allosterically enhances Ca²⁺ binding to sites I and II of WT and pathogenic calmodulin mutants bound to the channel CTD.