| Type: | Domain | Name: | GYF domain |
| Description: | The glycine-tyrosine-phenylalanine (GYF) domain is an around 60-amino acid domain which contains a conserved GP[YF]xxxx[MV]xxWxxx[GN]YF motif. It was identified in the human intracellular protein termed CD2 binding protein 2(CD2BP2), which binds to a site containing two tandem PPPGHR segments within the cytoplasmic region of CD2. Binding experiments and mutational analyseshave demonstrated the critical importance of the GYF tripeptide in ligand binding. A GYF domain is also found in several other eukaryotic proteins ofunknown function []. It has been proposed that the GYF domain found in theseproteins could also be involved in proline-rich sequence recognition [].Resolution of the structure of the CD2BP2 GYF domain by NMR spectroscopy revealed a compact domain with a beta-beta-alpha-beta-beta topology, where thesingle alpha-helix is tilted away from the twisted, anti-parallel beta-sheet. The conserved residues of the GYF domain create a contiguouspatch of predominantly hydrophobic nature which forms an integral part of the ligand-binding site []. There is limited homology within the C-terminal 20-30amino acids of various GYF domains, supporting the idea that this part of the domain is structurally but not functionally important []. | Short Name: | GYF |
