|
ИСТИНА |
Войти в систему Регистрация |
ИСТИНА ИНХС РАН |
||
One of the Ca2+ binding sites of recoverin exclusively controls interaction with rhodopsin kinaseстатья
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: Komolov K.E., Zinchenko D.V., Churumova V.A., Vaganova S.A., Weiergraber O.H., Senin I.I., Philippov P.P., Koch K.W.
- Журнал: Biological Chemistry
- Том: 386
- Номер: 3
- Год издания: 2005
- Издательство: Walter de Gruyter GmbH & Co. KG
- Местоположение издательства: Germany
- Первая страница: 285
- Последняя страница: 289
- DOI: 10.1515/BC.2005.034
- Аннотация: Recoverin is a neuronal calcium sensor protein that controls the activity of rhodopsin kinase in a Ca2+-dependent manner. Mutations in the EF-hand Ca2+ binding sites are valuable tools for investigating the functional properties of recoverin. In the recoverin mutant E121Q (ReCE121Q) the high-affinity Ca2+ binding site is disabled. The non-myristoylated form of ReCE121Q binds one Ca2+ via its second Ca2+ -binding site (EF-hand 2), whereas the myristoylated variant does not bind Ca2+ at all. Binding of Ca2+ to non-myristoylated ReCE121Q apparently triggers exposure of apolar side chains, allowing for association with hydrophobic matrices. Likewise, an interaction surface for the recoverin target rhodopsin kinase is constituted upon Ca2+ binding to the non-acylated mutant. Structural changes resulting from Ca2+-occupation of EF-hand 2 in myristoylated and non-myristoylated recoverin variants are discussed in terms of critical conditions required for biological activity.
- Добавил в систему: Филиппов Павел Павлович