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GYF Domain
Class:Pro-rich binding

No Image The GYF domain forms a unique bulge-helix-bulge motif in which a single a-helix is tilted away from a twisted, anti-parallel b-sheet. The poly-proline peptide binding site is believed to be a concave hydrophobic patch that winds across the molecular surface of the domain. To date, no co-structures with bound peptide exist to confirm peptide conformation in the binding pocket. The figure shows the structure of the GYF domain of CD2.

Structure Reference:
Freund, C. et al. (1999) Nat. Struct. Biol. 6(7): 656-60. PDB: 1GYF.

Domain binding and function:
 structure The glycine-tyrosine-phenylalanine, or GYF, domain was first reported in the CD2 binding protein CDBP2 as a domain capable of binding to a proline-rich peptide sequence in the CD2 tail region. Despite functioning as a proline-rich peptide binding domain, the GYF fold is structurally unrelated to the SH3 or WW domains. The GYF domain of CDBP2 binds to a PPPPGHR repeat in the CD2 tail via a relatively smooth, concave surface that forms a continuous hydrophobic patch containing many of the GYF domain conserved residues.
Examples of Proteins: 
GYF domain protein
Binding partner GYF domain binding site

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