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由约100个氨基酸残基组成的SH2结构域特异性识别配体上磷酸化酪氨酸及其C端的3～6个氨基酸残基。其对配体的识别特性取决于特定的空间结构。SH2结构域广泛存在于蛋白酪氨酸激酶、磷酸酶、磷酯酶、信号接头蛋白及转录因子等蛋白分子内,而参与调控相应的信号传导通路。SH2结构域所介导的信号通路的异常会导致多种遗传病及肿瘤的发生。因此对其配体识别特性的研究及相应的靶分子模拟物的研究受到生物学家及药学家的青睐。
The SH2 domain, consisting of approximately 100 amino acid residues, specifically recognizes phosphorylated tyrosine and 3 to 6 amino acid residues at its C-terminus. Its recognition of ligands depends on the specific spatial structure. SH2 domain exists widely in protein tyrosine kinases, phosphatases, phosphatases, signal adapter proteins and transcription factors and other protein molecules involved in the regulation of the corresponding signal transduction pathway. SH2 domain-mediated abnormalities in the signaling pathways lead to the development of a variety of genetic diseases and tumors. Therefore, the study of its ligand recognition properties and the corresponding target mimics have been favored by biologists and pharmacologists.