The structure of an FF domain from human HYPA/FBP11

J Mol Biol. 2002 Oct 25;323(3):411-6. 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 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Carrier Proteins / chemistry*
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Phosphopeptides / metabolism
  • Protein Binding
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Tertiary*
  • Sequence Alignment


  • Carrier Proteins
  • Phosphopeptides