title: The structure of an FF domain from human HYPA/FBP11.
abstract: The FF domain is a 60 amino acid residue phosphopeptide-binding module found in a variety of eukaryotic proteins including the transcription elongation factor CA150, the splicing factor Prp40 and p190RHOGAP. We have determined the structure of an FF domain from HYPA/FBP11. The domain is composed of three alpha helices arranged in an orthogonal bundle with a 3(10) helix in the loop between the second and third alpha helices. The structure differs from those of other phosphopeptide-binding domains and represents a novel phosphopeptide-binding fold.
authors.affiliation: MRC Centre for Protein Engineering, Cambridge, UK.
authors.forename: Mark
authors.initials: M
authors.lastname: Allen
authors.forename: Assaf
authors.initials: A
authors.lastname: Friedler
authors.forename: Oliver
authors.initials: O
authors.lastname: Schon
authors.forename: Mark
authors.initials: M
authors.lastname: Bycroft
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010748:Phosphopeptides / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment
chemical_list: D002352:Carrier Proteins; D010748:Phosphopeptides