The Structure of an FF Domain from Human HYPA/FBP11

• Published in: Journal of molecular biology Vol. 323; no. 3; pp. 411 - 416
• Main Authors: Allen, Mark, Friedler, Assaf, Schon, Oliver, Bycroft, Mark
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 25.10.2002
• Subjects: Amino Acid Sequence; Binding Sites; Carrier Proteins - chemistry; Carrier Proteins - genetics; Carrier Proteins - metabolism; Humans; Models, Molecular; Molecular Sequence Data; NMR structure; Nuclear Magnetic Resonance, Biomolecular; phosphopeptide recognition; Phosphopeptides - metabolism; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Tertiary; RNA polymerase II carboxyl-terminal domain; Sequence Alignment; transcription; CTD, carboxyl-terminal domain; NMR structure; RNA polymerase II carboxyl-terminal domain; transcription; phosphopeptide recognition; RNAP II, RNA polymerase II
• ISSN: 0022-2836; 1089-8638
• DOI: 10.1016/S0022-2836(02)00968-3

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 α helices arranged in an orthogonal bundle with a 3 10 helix in the loop between the second and third α helices. The structure differs from those of other phosphopeptide-binding domains and represents a novel phosphopeptide-binding fold.