3U21

Crystal structure of a Fragment of Nuclear factor related to kappa-B-binding protein (residues 370-495) (NFRKB) from Homo sapiens at 2.18 A resolution

Summary for 3U21

• Entry DOI: 10.2210/pdb3u21/pdb
• Descriptor: Nuclear factor related to kappa-B-binding protein, SODIUM ION (3 entities in total)
• Functional Keywords: dna/rna-binding 3-helical bundle, winged-hth domain, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-biology, transcription regulation, dna binding protein, dna binding, partnership for stem cell biology, stemcell
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus : Q6P4R8
• Total number of polymer chains: 2
• Total formula weight: 29031.18

Authors

Joint Center for Structural Genomics (JCSG),Partnership for Stem Cell Biology (STEMCELL) (deposition date: 2011-09-30, release date: 2011-11-02, Last modification date: 2025-10-22)

Primary citation

Kumar, A.,Mocklinghoff, S.,Yumoto, F.,Jaroszewski, L.,Farr, C.L.,Grzechnik, A.,Nguyen, P.,Weichenberger, C.X.,Chiu, H.J.,Klock, H.E.,Elsliger, M.A.,Deacon, A.M.,Godzik, A.,Lesley, S.A.,Conklin, B.R.,Fletterick, R.J.,Wilson, I.A.
Structure of a Novel Winged-Helix Like Domain from Human NFRKB Protein.
Plos One, 7:e43761-e43761, 2012

PubMed 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.

PubMed: 22984442
DOI: 10.1371/journal.pone.0043761

Experimental method

X-RAY DIFFRACTION (2.18 Å)