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PLoS One. 2012;7(9):e43761. doi: 10.1371/journal.pone.0043761. Epub 2012 Sep 11.

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

Author information

1
Joint Center for Structural Genomics, La Jolla, California, United States of America.

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.

PMID:
22984442
PMCID:
PMC3439487
DOI:
10.1371/journal.pone.0043761
[Indexed for MEDLINE]
Free PMC Article

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