Structure determinants defining the specificity of papain-like cysteine proteases

Авторы: Petushkova Anastasiia I., Savvateeva Lyudmila V., Zamyatnin Andrey A.
Журнал: Computational and Structural Biotechnology Journal
Том: 20
Год издания: 2022
Первая страница: 6552
Последняя страница: 6569
DOI: 10.1016/j.csbj.2022.11.040
Аннотация: Papain-like cysteine proteases are widely expressed enzymes that mostly regulate protein turnover in the acidic conditions of lysosomes. However, in the last twenty years, these proteases have been evidenced to exert specific functions within different organelles as well as outside the cell. The most studied proteases of this family are human cysteine cathepsins involved both in physiological and pathological processes. The specificity of each protease to its substrates is mostly defined by the structure of the binding cleft. Different patterns of amino acid motif in this area determine the interaction between the protease and the ligands. Moreover, this specificity can be altered under the specific media conditions and in case other proteins are present. Understanding how this network works would allow researchers to design the diagnostic selective probes and therapeutic inhibitors. Moreover, this knowledge might serve as a key for redesigning and de novo engineering of the proteases for a wide range of applications.
Добавил в систему: Замятнин Андрей Александрович

	ИСТИНА	Войти в систему Регистрация
	ИПМех РАН
	Главная Поиск Статистика О проекте Помощь

ИСТИНА