title: Structure of a novel winged-helix like domain from human NFRKB protein.
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.
authors.affiliation: Joint Center for Structural Genomics, La Jolla, California, United States of America.
authors.forename: Abhinav
authors.initials: A
authors.lastname: Kumar
authors.forename: Sabine
authors.initials: S
authors.lastname: Möcklinghoff
authors.forename: Fumiaki
authors.initials: F
authors.lastname: Yumoto
authors.forename: Lukasz
authors.initials: L
authors.lastname: Jaroszewski
authors.forename: Carol L
authors.initials: CL
authors.lastname: Farr
authors.forename: Anna
authors.initials: A
authors.lastname: Grzechnik
authors.forename: Phuong
authors.initials: P
authors.lastname: Nguyen
authors.forename: Christian X
authors.initials: CX
authors.lastname: Weichenberger
authors.forename: Hsiu-Ju
authors.initials: HJ
authors.lastname: Chiu
authors.forename: Heath E
authors.initials: HE
authors.lastname: Klock
authors.forename: Marc-André
authors.initials: MA
authors.lastname: Elsliger
authors.forename: Ashley M
authors.initials: AM
authors.lastname: Deacon
authors.forename: Adam
authors.initials: A
authors.lastname: Godzik
authors.forename: Scott A
authors.initials: SA
authors.lastname: Lesley
authors.forename: Bruce R
authors.initials: BR
authors.lastname: Conklin
authors.forename: Robert J
authors.initials: RJ
authors.lastname: Fletterick
authors.forename: Ian A
authors.initials: IA
authors.lastname: Wilson
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry; D018360:Crystallography, X-Ray; D044842:Cullin Proteins / Q000737:chemistry; D004247:DNA / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D011485:Protein Binding; D011489:Protein Denaturation; D060066:Protein Interaction Maps; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012097:Repressor Proteins / Q000737:chemistry; D012441:Saccharomyces cerevisiae / Q000737:chemistry; D016415:Sequence Alignment; D040681:Structural Homology, Protein; D013696:Temperature; D051540:Winged-Helix Transcription Factors / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; C100318:Cullin 1; D044842:Cullin Proteins; D004268:DNA-Binding Proteins; C101640:MecI protein, Staphylococcus; C072725:NFRKB protein, human; D012097:Repressor Proteins; D051540:Winged-Helix Transcription Factors; D004247:DNA