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Oligomeric structure of 14-3-3 protein: What do we know about monomers?статья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Авторы: Sluchanko N.N., Gusev N.B.
- Журнал: FEBS Letters
- Том: 586
- Номер: 24
- Год издания: 2012
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 4249
- Последняя страница: 4256
- DOI: 10.1016/j.febslet.2012.10.048.
- Аннотация: 14-3-3s predominantly form homo-/heterodimers that are in equilibrium with corresponding monomers. Dimer/monomer equilibrium depends on the nature and phosphorylation of Ser58 of certain 14-3-3 isoforms. The structure and properties of 14-3-3 dimers are well characterized, whereas 14-3-3 monomers are less investigated. Therefore design and analysis of dimer-incapable mutants of 14-3-3 are important. Truncated or heavily mutated proteins are not ideal since their structure may be distorted. Phosphomimicking mutations, such as S58(D/E), induce incomplete dimer dissociation. A recently characterized monomeric 14-3-3 contains few mutations and retains the original secondary structure. Monomeric 14-3-3 interacts with phosphorylated target proteins and has higher chaperone-like activity than dimeric 14-3-3. Further investigation of the properties of monomeric 14-3-3 is important for understanding its yet poorly characterized role in different cellular processes.
- Добавил в систему: Гусев Николай Борисович