Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2017 Apr 10;36(33):4673–4681. doi: 10.1038/onc.2017.60

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2017 The Author(s)

This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

PMC Copyright notice

Newly discovered c-NHEJ factor c9orf142/PAXX structurally resembles XRCC4. Figure shows computer models of XLF, XRCC4 and c9orf142/PAXX (adapted from Craxton et al., 2015). These proteins typically form dimers, however, here for simplicity and to highlight their structural similarity monomers are depicted. For XLF C-terminal portion of the coiled-coil has been shortened. The overall structure of a typical XRCC4 paralog includes a globular head domain, a centrally located coiled-coil and the C-terminal region (CTR, not shown). The CTRs are intrinsically disordered and not visible on available crystal structures. The head domain of XLF and XRCC4 is responsible for the formation of XLF/XRCC4 filaments, whereas the head domain of PAXX has an unknown function. The coiled-coils include regions necessary for dimerization. CTRs of XLF and PAXX mediate the interaction with Ku (not shown).