Campbell I D, Cooke R M, Baron M, Harvey T S, Tappin M J
Department of Biochemistry, University of Oxford, U.K.
Prog Growth Factor Res. 1989;1(1):13-22. doi: 10.1016/0955-2235(89)90038-0.
The structures of human epidermal growth factor (EGF) and human transforming growth factor alpha (TGF alpha) have been determined in solution using nuclear magnetic resonance techniques. The features of each structure are described and similarities and differences between them are discussed. The structures are combined with information from sequence homologies to produce a model of the receptor-recognition sites of EGF and TGF alpha, which can be tested in a site-directed mutagenesis programme. The model assists in explaining previous observations of sequence-activity relationships. The TGF alpha and EGF structures also serve as models for homologous modules in other extracellular proteins.
利用核磁共振技术已在溶液中确定了人表皮生长因子(EGF)和人转化生长因子α(TGFα)的结构。描述了每种结构的特征,并讨论了它们之间的异同。这些结构与来自序列同源性的信息相结合,以生成EGF和TGFα受体识别位点的模型,该模型可在定点诱变程序中进行测试。该模型有助于解释先前关于序列-活性关系的观察结果。TGFα和EGF结构还可作为其他细胞外蛋白中同源模块的模型。