Structure of a Novel Winged-Helix Like Domain from Human NFRKB Protein
- Kumar, Abhinav;
- Möcklinghoff, Sabine;
- Yumoto, Fumiaki;
- Jaroszewski, Lukasz;
- Farr, Carol L;
- Grzechnik, Anna;
- Nguyen, Phuong;
- Weichenberger, Christian X;
- Chiu, Hsiu-Ju;
- Klock, Heath E;
- Elsliger, Marc-André;
- Deacon, Ashley M;
- Godzik, Adam;
- Lesley, Scott A;
- Conklin, Bruce R;
- Fletterick, Robert J;
- Wilson, Ian A
- Editor(s): Vertessy, Beata G
- et al.
Published Web Location
https://doi.org/10.1371/journal.pone.0043761Abstract
The human nuclear factor related to kappa-B-binding protein (NFRKB) is a 1299-residue protein that is a component of the metazoan INO80 complex involved in chromatin remodeling, transcription regulation, DNA replication and DNA repair. Although full length NFRKB is predicted to be around 65% disordered, comparative sequence analysis identified several potentially structured sections in the N-terminal region of the protein. These regions were targeted for crystallographic studies, and the structure of one of these regions spanning residues 370-495 was determined using the JCSG high-throughput structure determination pipeline. The structure reveals a novel, mostly helical domain reminiscent of the winged-helix fold typically involved in DNA binding. However, further analysis shows that this domain does not bind DNA, suggesting it may belong to a small group of winged-helix domains involved in protein-protein interactions.
Many UC-authored scholarly publications are freely available on this site because of the UC's open access policies. Let us know how this access is important for you.