Review Version 1 Preserved in Portico This version is not peer-reviewed
Structural and Functional Insights into Human Nuclear Cyclophilins
Version 1 : Received: 31 October 2018 / Approved: 2 November 2018 / Online: 2 November 2018 (08:16:41 CET)
A peer-reviewed article of this Preprint also exists.
Rajiv, C.; Davis, T.L. Structural and Functional Insights into Human Nuclear Cyclophilins. Biomolecules 2018, 8, 161. Rajiv, C.; Davis, T.L. Structural and Functional Insights into Human Nuclear Cyclophilins. Biomolecules 2018, 8, 161.
The peptidyl-prolyl isomerases of the cyclophilin type are distributed throughout human cells, including eight found solely in the nucleus. Nuclear cyclophilins are involved in complexes that regulate chromatin modification, transcription, and pre-mRNA splicing. This review collects what is known about the eight human nuclear cyclophilins: PPIH, PPIE, PPIL1, PPIL2, PPIL3, PPIG, CWC27, and PPWD1. Each “spliceophilin” is evaluated in relation to the spliceosomal complex in which it has been studied, and current work studying the biological roles of these cyclophilins in the nucleus are discussed. All eight of the human splicing complexes available in the PDB are analyzed from the viewpoint of the human spliceophilins. Future directions in structural and cellular biology, and the importance of developing spliceophilin-specific inhibitors, are considered.
peptidyl-prolyl isomerases; nuclear cyclophilins; spliceophilins; alternative splicing; spliceosomes; NMR; X-ray crystallography
Biology and Life Sciences, Biochemistry and Molecular Biology
Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
We encourage comments and feedback from a broad range of readers. See criteria for comments and our Diversity statement.Leave a public comment
Send a private comment to the author(s)