CRYSTAL-STRUCTURE OF THE MAMMALIAN GRB2 ADAPTER
CRYSTAL-STRUCTURE OF THE MAMMALIAN GRB2 ADAPTER
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DOI：
10.1126/science.7716522
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发表时间：
1995-04-14
期刊：
影响因子：
56.9
通讯作者：
DUCRUIX, A
中科院分区：
文献类型：
--
作者：
MAIGNAN, S;GUILLOTEAU, JP;DUCRUIX, A
哺乳动物生长因子受体结合蛋白 Grb2 是介导 Ras 上鸟嘌呤核苷酸交换激活的接头。 Grb2 通过其 SH2 结构域与受体结合，并通过其两个 SH3 结构域与 Sevenless Son 的羧基末端结构域结合。因此，它是信号转导途径中的关键元件。 Grb2 的晶体结构确定为 3.1 埃分辨率。不对称单元由嵌入的二聚体组成。 SH2 和 SH3 结构域之间的交错连接使 SH3 结构域的两个相邻面形成范德华接触，但为富含脯氨酸的肽的结合留下了空间。
The mammalian growth factor receptor- binding protein Grb2 is an adaptor that mediates activation of guanine nucleotide exchange on Ras. Grb2 binds to the receptor through its SH2 domain and to the carboxyl-terminal domain of Son of sevenless through its two SH3 domains. It is thus a key element in the signal transduction pathway. The crystal structure of Grb2 was determined to 3.1 angstrom resolution. The asymmetric unit is composed of an embedded dimer. The interlaced junctions between the SH2 and SH3 domains bring the two adjacent faces of the SH3 domains in van der Waals contact but leave room for the binding of proline-rich peptides.