Freund C, Dötsch V, Nishizawa K, Reinherz E L, Wagner G
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Nat Struct Biol. 1999 Jul;6(7):656-60. doi: 10.1038/10712.
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.
通过CD2细胞表面受体激活T细胞是由其胞质尾部富含脯氨酸的序列传递的。一个参与细胞因子产生的膜近端富含脯氨酸的串联重复序列，被细胞内CD2结合蛋白CD2BP2识别。我们解析了CD2BP2的CD2结合结构域的溶液结构，我们将其命名为甘氨酸-酪氨酸-苯丙氨酸（GYF）结构域。GYF序列是一个结构独特的凸起-螺旋-凸起基序的一部分，该基序构成了CD2尾部的主要结合位点。一个疏水表面斑块由基序残基形成，这些残基在来自不同真核物种的多种蛋白质中高度保守。因此，GYF结构域的结构可能广泛用于蛋白质-蛋白质相互作用。
