1. Structure of a novel winged-helix like domain from human NFRKB protein.
- Author
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Kumar, Abhinav, Möcklinghoff, Sabine, Yumoto, Fumiaki, Jaroszewski, Lukasz, Farr, Carol L, Grzechnik, Anna, Nguyen, Phuong, Weichenberger, Christian X, Chiu, Hsiu-Ju, Klock, Heath E, Elsliger, Marc-André, Deacon, Ashley M, Godzik, Adam, Lesley, Scott A, Conklin, Bruce R, Fletterick, Robert J, and Wilson, Ian A
- Subjects
Humans ,Saccharomyces cerevisiae ,Cullin Proteins ,Bacterial Proteins ,DNA-Binding Proteins ,Repressor Proteins ,DNA ,Crystallography ,X-Ray ,Sequence Alignment ,Temperature ,Amino Acid Sequence ,Protein Structure ,Secondary ,Protein Structure ,Tertiary ,Structural Homology ,Protein ,Protein Binding ,Protein Denaturation ,Molecular Sequence Data ,Winged-Helix Transcription Factors ,Protein Interaction Maps ,Crystallography ,X-Ray ,Protein Structure ,Secondary ,Tertiary ,Structural Homology ,Protein ,Human Genome ,Genetics ,1.1 Normal biological development and functioning ,Generic Health Relevance ,General Science & Technology - 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.
- Published
- 2012