| Studies on Long-acting Insulin:Crystal Structure of Arg-B31 Human Insulin at 2.0 Resolution |
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| 作者姓名： | 任斌 王大成 常文瑞 张英 R.Obermeier |
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| 作者单位： | Institute of Biophysics，Academia Sinica，Beijing 100101，PRC，Institute of Biophysics，Academia Sinica，Beijing 100101，PRC，Institute of Biophysics，Academia Sinica，Beijing 100101，PRC，Institute of Biophysics，Academia Sinica，Beijing 100101，PRC，Pharma Forschung Biochemie，Hoechst AG，6230 Frankfurt am Main 80，FRG |
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| 基金项目： | Project supported by UNIDO Grant (91/048) and the High-Technology Program of China. |
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| 摘 要： | The crystal structure of Arg-B31 human insulin(ABHI), a long-acting insulin derivative, has been determined at 2.0 resolution by using X-ray diffraction analysis. The final crystallographic R factor of the structure model after the refinement is 0.189 with the bond length r. m. s deviation of 0.018 . The refined structure of ABHI showed that the conformation of B-chain C-terminal residues was more stable than that in the native molecule. A striking structural feature of ABHI was an additional ion pair formed between ArgB31 of molecule Ⅰ and Glu-B21 of molecule Ⅱ in a dimer, and three ionic bonds between the neighbouring molecules thereby appeared on the surface of ABHI hexamer.These secondary bonds generated by the insertion of the residue Arg-B31 should make the rate of dissociation of ABHI hexamer slow down when it was injected into the body and the property of protraction should be produced by a 'depot effect'. This ought to be the main structure basis of the prolonged action of ABHI. The results o
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