InterPro : IPR003169

Name  GYF Short Name  GYF
Type  Domain Description  The glycine-tyrosine-phenylalanine (GYF) domain is an around 60-amino aciddomain which contains a conserved GP[YF]xxxx[MV]xxWxxx[GN]YF motif. It wasidentified in the human intracellular protein termed CD2 binding protein 2(CD2BP2), which binds to a site containing two tandem PPPGHR segments withinthe cytoplasmic region of CD2. Binding experiments and mutational analyseshave demonstrated the critical importance of the GYF tripeptide in ligandbinding. 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 spectroscopyrevealed 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 theligand-binding site []. There is limited homology within the C-terminal 20-30amino acids of various GYF domains, supporting the idea that this part of thedomain is structurally but not functionally important [].
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InterPro protein domain ID --> Contigs

 

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3 Publications

First Author Title Year Journal Volume Pages
Nishizawa K Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation. 1998 Proc Natl Acad Sci U S A 95 14897-902
Freund C The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences. 1999 Nat Struct Biol 6 656-60
Freund C Dynamic interaction of CD2 with the GYF and the SH3 domain of compartmentalized effector molecules. 2002 EMBO J 21 5985-95



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)