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Structure of a novel winged-helix like domain from human NFRKB protein.

PloS one (2012-09-18)
Abhinav Kumar, Sabine Möcklinghoff, Fumiaki Yumoto, Lukasz Jaroszewski, Carol L Farr, Anna Grzechnik, Phuong Nguyen, Christian X Weichenberger, Hsiu-Ju Chiu, Heath E Klock, Marc-André Elsliger, Ashley M Deacon, Adam Godzik, Scott A Lesley, Bruce R Conklin, Robert J Fletterick, Ian A Wilson
ABSTRACT

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.