Global InformationGYF domain information
| GYF | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 the crystal structure of a binary u5 snrnp complex | |||||||||
| Identifiers | |||||||||
| Symbol | GYF | ||||||||
| Pfam | PF02213 | ||||||||
| InterPro | IPR003169 | ||||||||
| SMART | GYF | ||||||||
| SCOP2 | 1gyf / SCOPe / SUPFAM | ||||||||
| CDD | cd00072 | ||||||||
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In molecular biology, the GYF domain (glycine-tyrosine-phenylalanine domain) is an approximately 60-amino acid protein 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.[1] It has been proposed that the GYF domain found in these proteins could also be involved in proline-rich sequence recognition.[2] 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.[2] 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.[3]
- ^ Nishizawa K, Freund C, Li J, Wagner G, Reinherz EL (December 1998). "Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation". Proc. Natl. Acad. Sci. U.S.A. 95 (25): 14897–902. Bibcode:1998PNAS...9514897N. doi:10.1073/pnas.95.25.14897. PMC 24547. PMID 9843987.
- ^ a b Freund C, Dotsch V, Nishizawa K, Reinherz EL, Wagner G (July 1999). "The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences". Nat. Struct. Biol. 6 (7): 656–60. doi:10.1038/10712. PMID 10404223. S2CID 19688996.
- ^ Freund C, Kuhne R, Yang H, Park S, Reinherz EL, Wagner G (November 2002). "Dynamic interaction of CD2 with the GYF and the SH3 domain of compartmentalized effector molecules". EMBO J. 21 (22): 5985–95. doi:10.1093/emboj/cdf602. PMC 137194. PMID 12426371.