Molecular modeling of the tetramerization domain of human potassium channel Kv10.2 in different oligomeric states
- Авторы: Novoseletsky V.N.1, Volyntseva A.D.1, Shaitan K.V.1, Sokolova O.S.1
-
Учреждения:
- Department of Biology
- Выпуск: Том 72, № 2 (2017)
- Страницы: 69-73
- Раздел: Molecular Biology
- URL: https://journals.rcsi.science/0096-3925/article/view/173608
- DOI: https://doi.org/10.3103/S0096392517020031
- ID: 173608
Цитировать
Аннотация
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.
Об авторах
V. Novoseletsky
Department of Biology
Автор, ответственный за переписку.
Email: valeryns@gmail.com
Россия, Moscow, 119234
A. Volyntseva
Department of Biology
Email: valeryns@gmail.com
Россия, Moscow, 119234
K. Shaitan
Department of Biology
Email: valeryns@gmail.com
Россия, Moscow, 119234
O. Sokolova
Department of Biology
Email: valeryns@gmail.com
Россия, Moscow, 119234
Дополнительные файлы
