Campbell I D, Baron M, Cooke R M, Dudgeon T J, Fallon A, Harvey T S, Tappin M J
Department of Biochemistry, University of Oxford, U.K.
Biochem Pharmacol. 1990 Jul 1;40(1):35-40. doi: 10.1016/0006-2952(90)90175-k.
The solution structures of the homologous growth factors human epidermal growth factor (hEGF) and human transforming growth factor-alpha (hTGF-alpha), as determined by high resolution NMR and various computational methods, are described. Knowledge of these structures and the sequences of other homologous proteins leads to predictions about growth factor residues which may be involved in the receptor/ligand interface. Recent experiments designed to check these predictions are described briefly. These involve site-specific mutagenesis, receptor binding assays and high resolution NMR studies.
本文描述了通过高分辨率核磁共振(NMR)和各种计算方法测定的同源生长因子人表皮生长因子(hEGF)和人转化生长因子-α(hTGF-α)的溶液结构。了解这些结构以及其他同源蛋白的序列,可对可能参与受体/配体界面的生长因子残基进行预测。简要介绍了近期旨在验证这些预测的实验。这些实验包括位点特异性诱变、受体结合测定和高分辨率NMR研究。