Crystal structure of human epidermal growth factor and its dimerization
Crystal structure of human epidermal growth factor and its dimerization
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DOI：
10.1074/jbc.m102874200
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发表时间：
2001-09-14
影响因子：
4.8
通讯作者：
Bi, RC
中科院分区：
文献类型：
--
作者：
Lu, HS;Chai, JJ;Bi, RC
表皮生长因子(EGF)是一种典型的促生长多肽，通过与特定的细胞表面受体结合并诱导受体二聚化来发挥作用。目前对EGF诱导EGF受体二聚化的分子机制知之甚少。在pH值为8.1的条件下，测定了人表皮生长因子的晶体结构。在晶体的不对称单元中有两个人类EGF分子A和B，它们形成了一个潜在的二聚体。重要的是，许多已知的EGF与其受体结合所必需的残基参与了两个EGF分子之间的界面，这表明EGF二聚化在EGF诱导的受体二聚化过程中起着至关重要的作用。此外，EGF的晶体结构与在pH 2.0下测定的小鼠EGF的核磁共振结构的主要特征相同，但不同模型之间的结构比较揭示了EGF结构的新的细节特征和性质。
Epidermal growth factor (EGF) is a typical growth-stimulating peptide and functions by binding to specific cell-surface receptors and inducing dimerization of the receptors. Little is known about the molecular mechanism of EGF-induced dimerization of EGF receptors. The crystal structure of human EGF has been determined at pH 8.1. There are two human EGF molecules A and B in the asymmetric unit of the crystals, which form a potential dimer. Importantly, a number of residues known to be indispensable for EGF binding to its receptor are involved in the interface between the two EGF molecules, suggesting a crucial role of EGF dimerization in the EGF-induced dimerization of receptors. In addition, the crystal structure of EGF shares the main features of the NMR structure of mouse EGF determined at pH 2.0, but structural comparisons between different models have revealed new detailed features and properties of the EGF structure.