Pullen R A, Lindsay D G, Wood S P, Tickle I J, Blundell T L, Wollmer A, Krail G, Brandenburg D, Zahn H, Gliemann J, Gammeltoft S
Nature. 1976 Feb 5;259(5542):369-73. doi: 10.1038/259369a0.
X-ray analysis, circular dichroism, receptor binding and biological potencies of chemically modified insulins suggest that the conformation of the insulin molecule is critical to the formation of both the zinc insulin hexamer and the insulin-receptor complex. Results are consistent with an insulin receptor-binding region including many of the hydrophobic residues important to dimerisation in addition to more polar surface residues. There is a further possibility of formation of an antiparallel sheet structure between the insulin and receptor molecules in the complex similar to that between monomers in the insulin dimer.
X射线分析、圆二色性、受体结合以及化学修饰胰岛素的生物活性表明，胰岛素分子的构象对于锌胰岛素六聚体和胰岛素-受体复合物的形成至关重要。结果表明，胰岛素受体结合区域除了包括更多极性表面残基外，还包括许多对二聚化很重要的疏水残基。复合物中胰岛素与受体分子之间还有可能形成反平行片层结构，类似于胰岛素二聚体中单体之间的结构。
