Liang D C, Chang W R, Wang D C, Zhang J P
National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, PRC.
Sci China B. 1992 Apr;35(4):418-28.
The extensive conformational comparisons among the determined structures of the different species and crystal forms of insulin and the varied insulin derivatives were performed by using the least-squares superimposition technique and the graphics technique. The results of the investigation showed that the structure of molecule I in 2Zn insulin was closer to that of the natural monomer; the conformational difference between two molecules of a dimer came out during dimerization and it was further improved and stabilized during the hexamerization and packing of hexamers in crystal; through the hinge peptides, such as A10, B4, B8, B24, B20 and B23, there was a flexible relative motion among the structural segments in the insulin molecule, and the residues at the B-chain C-terminal might have a shift of more than 10A; the mobility for each residue side-chain was very different due to the different surroundings.
通过使用最小二乘叠加技术和图形技术，对胰岛素不同物种和晶体形式以及各种胰岛素衍生物的已确定结构进行了广泛的构象比较。研究结果表明，2Zn胰岛素中分子I的结构更接近天然单体；二聚体的两个分子之间的构象差异在二聚化过程中出现，并在六聚化和晶体中六聚体堆积过程中进一步改善和稳定；通过铰链肽，如A10、B4、B8、B24、B20和B23，胰岛素分子中的结构片段之间存在灵活的相对运动，并且B链C末端的残基可能有超过10埃的位移；由于周围环境不同，每个残基侧链的流动性差异很大。
