International Journal of Biochemistry, Biophysics & Molecular Biology

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Cyclophilins: The Structure and Functions of an Important Peptidyl-prolyl Isomerase

Received: 02 May 2019    Accepted: 05 June 2019    Published: 28 June 2019
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Abstract

Cyclophilins are a subgroup of highly conserved protein family immunophilins which are peptidyl-prolyl isomerases that interconvert between the cis and trans positions. They can act as chaperones in maintaining conformational quality control of proteomes. They are structurally conserved throughout evolution and have been found in mammals, plants, insects, fungi, and bacteria. They share a common fold architecture consisting of 8 antiparallel beta sheets and two alpha helices that pack against the sheets. They exist in the cellular compartment of most tissues and encode special functions. Intracellular Cyclophilins are secreted from cells in response to inflammatory stimuli and can mediate intercellular communication. Pro-inflammatory signals may be stimulated by extracellular Cyclophilin. Overexpression of Cyclophilins can contribute to pathological conditions. Cyclophilins are involved in the pathogenesis of viral infection, neurodegenerative diseases, ageing and cancer. Exhibiting several molecular functions, Cyclophilins can bind to cyclosporine and calcium-dependent ser/thr Calcineurin and has been used to describe the immunosuppressive action of cyclosporine. Cyclophilin can stabilize the cis-trans conformation transition state and speed up isomerization steps in protein folding. This process is important in the assembly of multiple domain proteins. Their existence as foldases and molecular chaperones enable them to be able to assist in the covalent folding or unfolding and the assembly or disassembly of other macromolecular structures.

DOI 10.11648/j.ijbbmb.20190401.11
Published in International Journal of Biochemistry, Biophysics & Molecular Biology (Volume 4, Issue 1, June 2019)
Page(s) 1-6
Creative Commons

This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.

Copyright

Copyright © The Author(s), 2024. Published by Science Publishing Group

Keywords

Cyclophilin, Peptidyl-prolyl Isomerase, Immunosuppressive, Isomerization

References
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Author Information
  • Laboratory of Computational Biology, School of Life Sciences, University of Science and Technology of China, Hefei, China

  • Department of Chemical Sciences, Olabisi Onabanjo University, Ago-iwoye, Nigeria

  • Department of Biomedical Engineering, School of Life Sciences, University of Science and Technology of China, Hefei, China

  • Laboratory of Cellular Dynamics, School of Life Sciences, University of Science and Technology of China, Hefei, China

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    Mukhtar Idris, Mujeebat Idris, Fadahunsi Adeola, Divine Mensah Sedzro. (2019). Cyclophilins: The Structure and Functions of an Important Peptidyl-prolyl Isomerase. International Journal of Biochemistry, Biophysics & Molecular Biology, 4(1), 1-6. https://doi.org/10.11648/j.ijbbmb.20190401.11

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    Mukhtar Idris; Mujeebat Idris; Fadahunsi Adeola; Divine Mensah Sedzro. Cyclophilins: The Structure and Functions of an Important Peptidyl-prolyl Isomerase. Int. J. Biochem. Biophys. Mol. Biol. 2019, 4(1), 1-6. doi: 10.11648/j.ijbbmb.20190401.11

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    AMA Style

    Mukhtar Idris, Mujeebat Idris, Fadahunsi Adeola, Divine Mensah Sedzro. Cyclophilins: The Structure and Functions of an Important Peptidyl-prolyl Isomerase. Int J Biochem Biophys Mol Biol. 2019;4(1):1-6. doi: 10.11648/j.ijbbmb.20190401.11

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  • @article{10.11648/j.ijbbmb.20190401.11,
      author = {Mukhtar Idris and Mujeebat Idris and Fadahunsi Adeola and Divine Mensah Sedzro},
      title = {Cyclophilins: The Structure and Functions of an Important Peptidyl-prolyl Isomerase},
      journal = {International Journal of Biochemistry, Biophysics & Molecular Biology},
      volume = {4},
      number = {1},
      pages = {1-6},
      doi = {10.11648/j.ijbbmb.20190401.11},
      url = {https://doi.org/10.11648/j.ijbbmb.20190401.11},
      eprint = {https://download.sciencepg.com/pdf/10.11648.j.ijbbmb.20190401.11},
      abstract = {Cyclophilins are a subgroup of highly conserved protein family immunophilins which are peptidyl-prolyl isomerases that interconvert between the cis and trans positions. They can act as chaperones in maintaining conformational quality control of proteomes. They are structurally conserved throughout evolution and have been found in mammals, plants, insects, fungi, and bacteria. They share a common fold architecture consisting of 8 antiparallel beta sheets and two alpha helices that pack against the sheets. They exist in the cellular compartment of most tissues and encode special functions. Intracellular Cyclophilins are secreted from cells in response to inflammatory stimuli and can mediate intercellular communication. Pro-inflammatory signals may be stimulated by extracellular Cyclophilin. Overexpression of Cyclophilins can contribute to pathological conditions. Cyclophilins are involved in the pathogenesis of viral infection, neurodegenerative diseases, ageing and cancer. Exhibiting several molecular functions, Cyclophilins can bind to cyclosporine and calcium-dependent ser/thr Calcineurin and has been used to describe the immunosuppressive action of cyclosporine. Cyclophilin can stabilize the cis-trans conformation transition state and speed up isomerization steps in protein folding. This process is important in the assembly of multiple domain proteins. Their existence as foldases and molecular chaperones enable them to be able to assist in the covalent folding or unfolding and the assembly or disassembly of other macromolecular structures.},
     year = {2019}
    }
    

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    AU  - Mukhtar Idris
    AU  - Mujeebat Idris
    AU  - Fadahunsi Adeola
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    JF  - International Journal of Biochemistry, Biophysics & Molecular Biology
    JO  - International Journal of Biochemistry, Biophysics & Molecular Biology
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    PB  - Science Publishing Group
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    AB  - Cyclophilins are a subgroup of highly conserved protein family immunophilins which are peptidyl-prolyl isomerases that interconvert between the cis and trans positions. They can act as chaperones in maintaining conformational quality control of proteomes. They are structurally conserved throughout evolution and have been found in mammals, plants, insects, fungi, and bacteria. They share a common fold architecture consisting of 8 antiparallel beta sheets and two alpha helices that pack against the sheets. They exist in the cellular compartment of most tissues and encode special functions. Intracellular Cyclophilins are secreted from cells in response to inflammatory stimuli and can mediate intercellular communication. Pro-inflammatory signals may be stimulated by extracellular Cyclophilin. Overexpression of Cyclophilins can contribute to pathological conditions. Cyclophilins are involved in the pathogenesis of viral infection, neurodegenerative diseases, ageing and cancer. Exhibiting several molecular functions, Cyclophilins can bind to cyclosporine and calcium-dependent ser/thr Calcineurin and has been used to describe the immunosuppressive action of cyclosporine. Cyclophilin can stabilize the cis-trans conformation transition state and speed up isomerization steps in protein folding. This process is important in the assembly of multiple domain proteins. Their existence as foldases and molecular chaperones enable them to be able to assist in the covalent folding or unfolding and the assembly or disassembly of other macromolecular structures.
    VL  - 4
    IS  - 1
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