Cargando…
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...
Autores principales: | , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Research Network of Computational and Structural Biotechnology
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9712828/ https://www.ncbi.nlm.nih.gov/pubmed/36467578 http://dx.doi.org/10.1016/j.csbj.2022.11.040 |
_version_ | 1784841875987890176 |
---|---|
author | Petushkova, Anastasiia I. Savvateeva, Lyudmila V. Zamyatnin, Andrey A. |
author_facet | Petushkova, Anastasiia I. Savvateeva, Lyudmila V. Zamyatnin, Andrey A. |
author_sort | Petushkova, Anastasiia I. |
collection | PubMed |
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. |
format | Online Article Text |
id | pubmed-9712828 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Research Network of Computational and Structural Biotechnology |
record_format | MEDLINE/PubMed |
spelling | pubmed-97128282022-12-02 Structure determinants defining the specificity of papain-like cysteine proteases Petushkova, Anastasiia I. Savvateeva, Lyudmila V. Zamyatnin, Andrey A. Comput Struct Biotechnol J Review 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. Research Network of Computational and Structural Biotechnology 2022-11-24 /pmc/articles/PMC9712828/ /pubmed/36467578 http://dx.doi.org/10.1016/j.csbj.2022.11.040 Text en © 2022 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Review Petushkova, Anastasiia I. Savvateeva, Lyudmila V. Zamyatnin, Andrey A. Structure determinants defining the specificity of papain-like cysteine proteases |
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 | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9712828/ https://www.ncbi.nlm.nih.gov/pubmed/36467578 http://dx.doi.org/10.1016/j.csbj.2022.11.040 |
work_keys_str_mv | AT petushkovaanastasiiai structuredeterminantsdefiningthespecificityofpapainlikecysteineproteases AT savvateevalyudmilav structuredeterminantsdefiningthespecificityofpapainlikecysteineproteases AT zamyatninandreya structuredeterminantsdefiningthespecificityofpapainlikecysteineproteases |