Dafgård E, Bajaj M, Honegger A M, Pitts J, Wood S, Blundell T
J Cell Sci Suppl. 1985;3:53-64. doi: 10.1242/jcs.1985.supplement_3.6.
The insulin-like growth factors and hystricomorph insulins have been modelled by interactive computer graphics on the assumption that their sequence homology to insulin implies that they will have a similar tertiary structure. These studies suggest that, although the insulin-related molecules can adopt the insulin fold, they are unlikely to form hexamers and if they form dimers they will be of reduced stability. The non-suppressibility of insulin-like growth factors by anti-insulin antibodies is explained in terms of differences of surface residues in the region A8-A10 and B1-B5. Receptor affinity of insulins and insulin-like growth factors for insulin receptors is explicable in terms of a receptor-binding site in the vicinity of B25 Phe on the insulin surface. An equivalent region around B25 Tyr of insulin-like growth factors may be responsible for their binding to type 1 receptors, although binding type 2 receptors must involve a different surface region not shared by insulin.
基于胰岛素样生长因子和豪猪型胰岛素与胰岛素的序列同源性意味着它们将具有相似的三级结构这一假设，通过交互式计算机图形技术对其进行了建模。这些研究表明，尽管胰岛素相关分子可以采用胰岛素折叠结构，但它们不太可能形成六聚体，并且如果形成二聚体，其稳定性也会降低。抗胰岛素抗体对胰岛素样生长因子的不可抑制性可以通过A8 - A10区域和B1 - B5区域表面残基的差异来解释。胰岛素和胰岛素样生长因子对胰岛素受体的受体亲和力可以根据胰岛素表面B25苯丙氨酸附近的受体结合位点来解释。胰岛素样生长因子B25酪氨酸周围的等效区域可能负责它们与1型受体的结合，尽管与2型受体的结合必然涉及胰岛素不共有的不同表面区域。
