Solution NMR assignment of the C-terminal domain of human chTOG.

Biomol NMR Assign

Cardiovascular and Randall Division, King's College London, Guy's Campus, London, SE1 1UL, UK.

Published: October 2018

AI Article Synopsis

  • The protein chTOG (also known as CKAP5) is crucial for organizing the cellular structure, specifically for assembling k-fibres during cell division.
  • Recent research identified two new domains in chTOG's C-terminus: a cryptic TOG domain (TOG6) and a smaller helical domain, which are important for its interactions with other proteins during k-fibre assembly.
  • The NMR analysis of the chTOG C-terminal domain confirmed its structure primarily consists of α-helices, but also revealed significant unstructured and flexible segments within the protein.

Article 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 H-N HSQC spectrum is indicative of the presence of a considerable amount of unstructured and possibly flexible portions of protein in the domain.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6132821PMC
http://dx.doi.org/10.1007/s12104-018-9812-9DOI Listing

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