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Structure of a Novel Winged-Helix Like Domain from Human NFRKB Protein

  • Author(s): Kumar, A
  • Möcklinghoff, S
  • Yumoto, F
  • Jaroszewski, L
  • Farr, CL
  • Grzechnik, A
  • Nguyen, P
  • Weichenberger, CX
  • Chiu, HJ
  • Klock, HE
  • Elsliger, MA
  • Deacon, AM
  • Godzik, A
  • Lesley, SA
  • Conklin, BR
  • Fletterick, RJ
  • Wilson, IA
  • et al.

Published Web Location

https://doi.org/10.1371/journal.pone.0043761
No data is associated with this publication.
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. © 2012 Kumar et al.

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This item is under embargo until December 31, 2999.