1GYF
GYF DOMAIN FROM HUMAN CD2BP2 PROTEIN
Summary for 1GYF
| Entry DOI | 10.2210/pdb1gyf/pdb |
| Descriptor | PROTEIN (CYTOPLASMIC DOMAIN BINDING PROTEIN (CD2BP2)) (1 entity in total) |
| Functional Keywords | t cell signaling, proline-rich sequence recognition, adapter domain, immune system |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 7320.01 |
| Authors | Freund, C.,Doetsch, V.,Nishizawa, K.,Reinherz, E.L.,Wagner, G. (deposition date: 1999-04-30, release date: 2000-01-05, Last modification date: 2023-12-27) |
| Primary citation | Freund, C.,Dotsch, V.,Nishizawa, K.,Reinherz, E.L.,Wagner, G. The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences. Nat.Struct.Biol., 6:656-660, 1999 Cited by PubMed Abstract: T cell activation through the CD2 cell surface receptor is transmitted by proline-rich sequences within its cytoplasmic tail. A membrane-proximal proline-rich tandem repeat, involved in cytokine production, is recognized by the intracellular CD2 binding protein CD2BP2. We solved the solution structure of the CD2 binding domain of CD2BP2, which we name the glycine-tyrosine-phenylalanine (GYF) domain. The GYF sequence is part of a structurally unique bulge-helix-bulge motif that constitutes the major binding site for the CD2 tail. A hydrophobic surface patch is created by motif residues that are highly conserved among a variety of proteins from diverse eukaryotic species. Thus, the architecture of the GYF domain may be widely used in protein-protein associations. PubMed: 10404223DOI: 10.1038/10712 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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