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Three-Finger Proteins from the Ly6/uPAR Family: Functional Diversity within One Structural Motifстатья
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: 10 февраля 2018 г.
- Авторы: Vasilyeva N.A., Loktyushov E.V., Bychkov M.L., Shenkarev Z.O., Lyukmanova E.N.
- Журнал: Biochemistry (Moscow)
- Том: 82
- Номер: 13
- Год издания: 2017
- Издательство: Pleiades Publishing, Ltd
- Местоположение издательства: Road Town, United Kingdom
- Первая страница: 1702
- Последняя страница: 1715
- DOI: 10.1134/S0006297917130090
- Аннотация: —The discovery in higher animals of proteins from the Ly6/uPAR family, which have structural homology with snake “threefinger” neurotoxins, has generated great interest in these molecules and their role in the functioning of the organism. These proteins have been found in the nervous, immune, endocrine, and reproductive systems of mammals. There are two types of the Ly6/uPAR proteins: those associated with the cell membrane by GPIanchor and secreted ones. For some of them (Lynx1, SLURP1, SLURP2, Lypd6), as well as for snake αneurotoxins, the target of action is nico tinic acetylcholine receptors, which are widely represented in the central and peripheral nervous systems, and in many other tissues, including epithelial cells and the immune system. However, the targets of most proteins from the Ly6/uPAR family and the mechanism of their action remain unknown. This review presents data on the structural and functional properties of the Ly6/uPAR proteins, which reveal a variety of functions within a single structural motif.
- Добавил в систему: Васильева Наталья Александровна