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Structure determination of the C-terminal domain of human polypeptide release factor eRF-1 by NMR spectroscopyтезисы доклада
- Авторы: Mantsyzov A.B., Ivanova E.V., Birdsall B., Kolosov P.M., Kisselev L.L., Polshakov V.I.
- Сборник: The proceedings of the International Conference “Advances in NMR of protein and nucleic acid molecular recognition"
- Тезисы
- Год издания: 2008
- Место издания: Murnau, Germany
- Первая страница: 89
- Последняя страница: 89
- Аннотация: The termination of the protein biosynthesis on the ribosome has complex mechanism. Eukaryotic class-1 release factor (eRF1) plays a key role in this process. Protein consist of three domains. While roles of the N and M domains are well confirmed, the mechanism of eRF1 regulation via C-domain remains unclear. New structural information may help to clarify details of the mechanism of eRF1 regulation. Presented results of NMR signal assignments of the C-terminal domain of eRF1.
- Добавил в систему: Польшаков Владимир Иванович