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Point amino acid substitutions in the Ca2+-binding sites of recoverin. II. The unusual behavior of the protein upon the binding of calcium ionsстатья
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: Uversky V.N., Permyakov S.E., Senin I.I., Cherskaya A.M., Shulga-Morskoy S.V., Zinchenko D.V., Alekseev A.M., Zargarov A.A., Lipkin V.M., Philippov P.P., Permyakov E.A.
- Журнал: Bioorganicheskaya Khimiya
- Том: 26
- Номер: 3
- Год издания: 2000
- Издательство: Izdatel'stva Nauka
- Местоположение издательства: Russian Federation
- Первая страница: 173
- Последняя страница: 178
- Аннотация: The structural properties of myristoylated forms of recombinant recoverin of the wild type and of its mutants with damaged second and/or third Ca2+-binding sites were studied by fluorimetry and circular dichroism. The interaction of wild-type recoverin with calcium ions was shown to induce unusual structural rearrangements in its molecule. In particular, protein binding with Ca2+ ions results in an increase in the mobility of the environment of Trp residues, in higher hydrophobicity, and in elevated thermal stability (its thermal transition shifts by 15 degrees C to higher temperatures) but has almost no effect on its secondary structure. Similar structural changes induced by Ca2+ are also characteristic of the -EF2 mutant of recoverin whose second Ca2+-binding site is modified and cannot bind calcium ions. The structural properties of the -EF3 and -EF2,3 mutants (whose third or simultaneously second and third Ca2+-binding sites, respectively, are modified and damaged) are practically indifferent to calcium ions.
- Добавил в систему: Филиппов Павел Павлович