Structure determinants defining the specificity of papain-like cysteine proteases
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 mos...
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| Format: | Article |
| Language: | English |
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Elsevier
2022-01-01
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| Series: | Computational and Structural Biotechnology Journal |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2001037022005347 |
| _version_ | 1828087928817975296 |
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| author | Anastasiia I. Petushkova Lyudmila V. Savvateeva Andrey A. Zamyatnin, Jr |
| author_facet | Anastasiia I. Petushkova Lyudmila V. Savvateeva Andrey A. Zamyatnin, Jr |
| author_sort | Anastasiia I. Petushkova |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-11T05:19:02Z |
| format | Article |
| id | doaj.art-f3ec7f46add54acbbed3ffe6d904f648 |
| institution | Directory Open Access Journal |
| issn | 2001-0370 |
| language | English |
| last_indexed | 2024-04-11T05:19:02Z |
| publishDate | 2022-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Computational and Structural Biotechnology Journal |
| spelling | doaj.art-f3ec7f46add54acbbed3ffe6d904f6482022-12-24T04:55:19ZengElsevierComputational and Structural Biotechnology Journal2001-03702022-01-012065526569Structure determinants defining the specificity of papain-like cysteine proteasesAnastasiia I. Petushkova0Lyudmila V. Savvateeva1Andrey A. Zamyatnin, Jr2Institute of Molecular Medicine, Sechenov First Moscow State Medical University, 8-2 Trubetskaya Str, 119991 Moscow, Russia; Sirius University of Science and Technology, 1 Olimpiysky pr-t, 354340 Sochi, RussiaInstitute of Molecular Medicine, Sechenov First Moscow State Medical University, 8-2 Trubetskaya Str, 119991 Moscow, RussiaInstitute of Molecular Medicine, Sechenov First Moscow State Medical University, 8-2 Trubetskaya Str, 119991 Moscow, Russia; Sirius University of Science and Technology, 1 Olimpiysky pr-t, 354340 Sochi, Russia; Belozersky Institute of Physico Chemical Biology, Lomonosov Moscow State University, 1-40 Leninskye gory, 119992 Moscow, Russia; Faculty of Health and Medical Sciences, University of Surrey, Guildford GU2 7X, UK; Corresponding author at: Institute of Molecular Medicine, Sechenov First Moscow State Medical University, 8-2 Trubetskaya Str, 119991 Moscow, Russia.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.http://www.sciencedirect.com/science/article/pii/S2001037022005347Papain-like cysteine proteaseCysteine cathepsinProtease specificityBinding siteSelective inhibitorProtein engineering |
| spellingShingle | Anastasiia I. Petushkova Lyudmila V. Savvateeva Andrey A. Zamyatnin, Jr Structure determinants defining the specificity of papain-like cysteine proteases Computational and Structural Biotechnology Journal Papain-like cysteine protease Cysteine cathepsin Protease specificity Binding site Selective inhibitor Protein engineering |
| title | Structure determinants defining the specificity of papain-like cysteine proteases |
| title_full | Structure determinants defining the specificity of papain-like cysteine proteases |
| title_fullStr | Structure determinants defining the specificity of papain-like cysteine proteases |
| title_full_unstemmed | Structure determinants defining the specificity of papain-like cysteine proteases |
| title_short | Structure determinants defining the specificity of papain-like cysteine proteases |
| title_sort | structure determinants defining the specificity of papain like cysteine proteases |
| topic | Papain-like cysteine protease Cysteine cathepsin Protease specificity Binding site Selective inhibitor Protein engineering |
| url | http://www.sciencedirect.com/science/article/pii/S2001037022005347 |
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