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Molecular dynamics simulation confirmed the stability of dimeric, trimeric, and tetrameric forms of the human Kv10.2 C-terminal domain and identified structure-stabilizing interactions.
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Molecular modeling confirmed the stability of different oligomeric states of the human Kv10.2 potassium channel tetramerization domain, providing insights into its spatial structure.
A voltage-gated potassium channel Kv10.2 is expressed in the nervous system, but its functions and involvement in the development of human disease remain poorly understood. Mutant forms of the Kv10.2 channel were found in patients with epileptic encephalopathy and autism. Molecular modeling of the channel spatial structure is an important tool for gaining knowledge about the molecular aspects of the channel functioning and mechanisms responsible for pathogenesis. In the present work, molecular modeling of the helical fragment of the human Kv10.2 (hEAG2) C-terminal domain in dimeric, trimeric, and tetrameric forms was performed. The stability of all forms was confirmed by molecular dynamics simulation. Contacts and interactions, stabilizing the structure, were identified.
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Novoseletsky et al. (2017) studied this question. Molecular modeling and dynamics simulation of human Kv10.2 C-terminal domain was evaluated on Stability of dimeric, trimeric, and tetrameric forms and identification of stabilizing contacts. Molecular dynamics simulation confirmed the stability of dimeric, trimeric, and tetrameric forms of the human Kv10.2 C-terminal domain and identified structure-stabilizing interactions.
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