标题：Conformational characterization of a single-site mutant of murine epidermal growth factor (EGF) by 1H NMR provides evidence that leucine-47 is involved in the interactions with the EGF receptor
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1989
卷号：86
期号：24
页码：9836-9840
DOI：10.1073/pnas.86.24.9836
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Epidermal growth factor (EGF) is a small protein containing 53 amino acids and three disulfide bonds. There is significant current interest in structure-function relationships in EGF and EGF-like proteins, including the homologous type-alpha transforming growth factors. The Leu-47 residue of murine EGF (mEGF) is one of several that are strongly conserved among the EGF-like growth factors, suggesting that it may contribute to the active site of mEGF. In several different binding assays, the activity of the mutant analog in which Leu-47 is replaced by Ser [( Ser47]mEGF) ranges from 8 to 18 times weaker than that of wild-type mEGF. The NMR data summarized in this paper demonstrate that the significant differences in the binding activities of wild-type and [Ser47]mEGF cannot be attributed to structural changes remote from the three-dimensional site of mutation. The only minor conformational changes that are indicated by these data involve side chains of residues proximal to Leu-47 in the three-dimensional structure. Therefore, Leu-47 and/or residues spatially adjacent to Leu-47 constitute part of the active site of mEGF.
