Article: Structure determinants defining the specificity of papain-like cysteine proteases.
Computational and structural biotechnology journal
2022 Volume 20, Page(s) 6552–6569
Abstract: 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 ... ...
Abstract | 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 |
---|---|
Language | English |
Publishing date | 2022-11-24 |
Publishing country | Netherlands |
Document type | Journal Article ; Review |
ZDB-ID | 2694435-2 |
ISSN | 2001-0370 |
ISSN | 2001-0370 |
DOI | 10.1016/j.csbj.2022.11.040 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
Full text online
More links
Kategorien
Order via subito
This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.