Rostkova, E, Burgess, SG, Bayliss, R orcid.org/0000-0003-0604-2773 et al. (1 more author) (2018) Solution NMR assignment of the C-terminal domain of human chTOG. Biomolecular NMR Assignments, 12 (2). pp. 221-224. ISSN 1874-2718
Abstract
The microtubule regulatory protein colonic and hepatic tumor overexpressed gene (chTOG), also known as cytoskeleleton associated protein 5 (CKAP5) plays an important role in organizing the cytoskeleton and in particular in the assembly of k-fibres in mitosis. Recently, we dissected the hitherto poorly understood C-terminus of this protein by discovering two new domains—a cryptic TOG domain (TOG6) and a smaller, helical domain at the very C-terminus. It was shown that the C-terminal domain is important for the interaction with the TACC domain in TACC3 during the assembly of k-fibres in a ternary complex that also includes clathrin. Here we now present the solution NMR assignment of the chTOG C-terminal domain which confirms our earlier prediction that it is mainly made of α-helices. However, the appearance of the 1H–15N HSQC spectrum is indicative of the presence of a considerable amount of unstructured and possibly flexible portions of protein in the domain.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2018, The Author(s). This article is 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, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
Keywords: | Mitosis; Kinetochore; TACC3; ChTOG; Cell cycle |
Dates: |
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Institution: | The University of Leeds |
Depositing User: | Symplectic Publications |
Date Deposited: | 18 Apr 2018 12:48 |
Last Modified: | 25 Jun 2023 21:18 |
Status: | Published |
Publisher: | Springer Verlag |
Identification Number: | 10.1007/s12104-018-9812-9 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:129755 |
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