 GYF Domain | |
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| Class:Pro-rich binding | |
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Structure:
 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.
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Domain binding and function:
 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.
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Examples of Proteins:
| GYF domain protein |
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Binding partner |
GYF domain binding site |
| CDBP2 |  |
CD2 |
PPPPGHR |
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Referenced in part on Cell Signaling Technology Website, Reference Section on Protein Domains. We gratefully acknowledge the following contributors:
Piers Nash1, Dan Lin3, Kathleen Binns2, Clark Wells2, Rob Ingham2, Terry Kubiseski2, Bernard Liu1, Matt Smith2,3, Ivan Blasutig2,3, Maria Sierra1, Caesar Lim2,3, Michael Arc1, Jim Fawcett2 and Tony Pawson2,3.
1. Ben May Institute for Cancer Research, The University of Chicago, Chicago, Illinois, 60637, USA
2. Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, M5G 1X5, Canada
3. Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario, M5S 1A8, Canada
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