GYFContains conserved Gly-Tyr-Phe residues
|SMART accession number:||SM00444|
|Description:||Proline-binding domain in CD2-binding protein. Contains conserved Gly-Tyr-Phe residues.|
|Interpro abstract (IPR003169):|
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 analyses have demonstrated the critical importance of the GYF tripeptide in ligand binding. A GYF domain is also found in several other eukaryotic proteins of unknown function [(PUBMED:9843987)]. It has been proposed that the GYF domain found in these proteins could also be involved in proline-rich sequence recognition [(PUBMED:10404223)]. 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 the single alpha-helix is tilted away from the twisted, anti-parallel beta-sheet. The conserved residues of the GYF domain create a contiguous patch of predominantly hydrophobic nature which forms an integral part of the ligand-binding site [(PUBMED:10404223)]. There is limited homology within the C-terminal 20-30 amino acids of various GYF domains, supporting the idea that this part of the domain is structurally but not functionally important [(PUBMED:12426371)].
|GO function:||protein binding (GO:0005515)|
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