Volume 4, Issue 1, June 2019, Page: 1-6
Cyclophilins: The Structure and Functions of an Important Peptidyl-prolyl Isomerase
Mukhtar Idris, Laboratory of Computational Biology, School of Life Sciences, University of Science and Technology of China, Hefei, China
Mujeebat Idris, Department of Chemical Sciences, Olabisi Onabanjo University, Ago-iwoye, Nigeria
Fadahunsi Adeola, Department of Biomedical Engineering, School of Life Sciences, University of Science and Technology of China, Hefei, China
Divine Mensah Sedzro, Laboratory of Cellular Dynamics, School of Life Sciences, University of Science and Technology of China, Hefei, China
Received: May 2, 2019;       Accepted: Jun. 5, 2019;       Published: Jun. 28, 2019
DOI: 10.11648/j.ijbbmb.20190401.11      View  689      Downloads  150
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.
Cyclophilin, Peptidyl-prolyl Isomerase, Immunosuppressive, Isomerization
To cite this article
Mukhtar Idris, Mujeebat Idris, Fadahunsi Adeola, Divine Mensah Sedzro, Cyclophilins: The Structure and Functions of an Important Peptidyl-prolyl Isomerase, International Journal of Biochemistry, Biophysics & Molecular Biology. Vol. 4, No. 1, 2019, pp. 1-6. doi: 10.11648/j.ijbbmb.20190401.11
Copyright © 2019 Authors retain the copyright of this article.
This article is an open access article distributed under the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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