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The structural mechanism of KCNH-channel regulation by the eag domain.

Nature · 2013 · PMC3910112 · PMID 23975098

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an unexpected trendno p-value reported
When we mapped the positions of disease-causing mutations in KCNH channels onto the structure of the eag domain-CNBHD complex, an unexpected trend emerged: many LQT2 mutations (at homologous positions in hERG1) and cancer-associated mutations (in hEAG1) are located at the interface between the eag domain and CNBHD ( Fig. 1c , supplementary Fig. 4 ).

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