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. © 2012 Kumar et al.
CITATION STYLE
Kumar, A., Möcklinghoff, S., Yumoto, F., Jaroszewski, L., Farr, C. L., Grzechnik, A., … Wilson, I. A. (2012). Structure of a Novel Winged-Helix Like Domain from Human NFRKB Protein. PLoS ONE, 7(9). https://doi.org/10.1371/journal.pone.0043761
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