Solution structure of the SH3 domain of Src and identification of its ligand-binding site.
Solution structure of the SH3 domain of Src and identification of its ligand-binding site.
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DOI：
10.1126/science.1280858
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发表时间：
1992-12
期刊：
影响因子：
56.9
通讯作者：
Hongtao Yu;M. Rosen;Tae Bum Shin;C. Seidel-Dugan;J. Brugge;S. Schreiber
中科院分区：
文献类型：
--
作者：
Hongtao Yu;M. Rosen;Tae Bum Shin;C. Seidel-Dugan;J. Brugge;S. Schreiber
Src 同源 3 (SH3) 区域是一个由 55 至 75 个氨基酸组成的蛋白质结构域，存在于许多细胞质蛋白中，包括那些参与信号转导途径的蛋白。通过多维核磁共振方法测定了酪氨酸激酶Src的SH3结构域的溶液结构。该分子由两条短的三链反平行β片层以近似直角堆积在一起组成。对与富含脯氨酸的肽配体结合的 SH3 结构域的研究揭示了蛋白质表面上的疏水性结合位点，该位点排列有保守的芳香族氨基酸的侧链。
The Src homology 3 (SH3) region is a protein domain of 55 to 75 amino acids found in many cytoplasmic proteins, including those that participate in signal transduction pathways. The solution structure of the SH3 domain of the tyrosine kinase Src was determined by multidimensional nuclear magnetic resonance methods. The molecule is composed of two short three-stranded anti-parallel beta sheets packed together at approximately right angles. Studies of the SH3 domain bound to proline-rich peptide ligands revealed a hydrophobic binding site on the surface of the protein that is lined with the side chains of conserved aromatic amino acids.