1gyf
From Proteopedia
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GYF DOMAIN FROM HUMAN CD2BP2 PROTEIN
Overview
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.
About this Structure
1GYF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences., Freund C, Dotsch V, Nishizawa K, Reinherz EL, Wagner G, Nat Struct Biol. 1999 Jul;6(7):656-60. PMID:10404223
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