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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >The structure of T(6) bovine insulin.
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The structure of T(6) bovine insulin.

机译：T(6)牛胰岛素的结构。

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Porcine insulin differs in sequence from bovine insulin at residues A8 (Thr in porcine-->Ala in bovine) and A10 (Ile in porcine-->Val in bovine). The structure of T(6) hexameric bovine insulin has been determined to 2.25 A resolution at room temperature and refined to a residual of 0.162. The structure of the independent dimer is nearly identical to the T(6) porcine insulin dimer: the mean displacement of all backbone atoms is 0.16 A, with the largest displacements occurring at AlaB30. Each of two independent zinc ions is octahedrally coordinated by three HisB10 side chains and three water molecules. As has been observed in both human and porcine insulin, the GluB13 side chains are directed towards the center of the hexamer, where a short contact of 2.57 A occurs between two independent carboxyl O atoms, again suggesting the presence of a centered hydrogen bond. No significant displacements of backbone atoms or changes in conformation are observed at A8 or A10. Since there are no interhexamer hydrogen-bonded contacts involving A8 in either porcine or bovine insulin, the change in the identity of this residue appears to have little or no effect upon the packing of the hexamers in the unit cell. In contrast, the side chains of the three A10 residues in one trimer make van der Waals contacts with the A10 side chains in a translationally related hexamer. As a consequence of the loss of the C(delta1) atom from the isoleucine residue in porcine insulin to produce valine in bovine insulin, there is a 0.36 A decrease in the distance between independent pairs of C(beta) atoms and a 0.24 A decrease in the c dimension of the unit cell. Thus, the net effect of the change in sequence at A10 is to strengthen the stabilizing hydrophobic interactions between hexamers.
机译：从牛猪胰岛素不同序列胰岛素在残留A8(刺猪——>阿拉巴马州在猪牛)和A10 (Ile——> Val牛)。T的结构(6)hexameric牛胰岛素2.25已决心决议在房间吗0.162温度和精制的残余。独立的二聚体的结构是近的相同的T(6)猪胰岛素二聚体:骨架原子的位移均值为0.16一个,最大位移发生在AlaB30。八面体的协调由三个HisB10一边链和三个水分子。观察到在人类和猪胰岛素,GluB13侧链都指向六聚体的中心,短暂的接触发生在两个独立的羧基之间2.57 O原子,再次暗示的存在为中心的氢键。骨架原子的位移或变化构象是观察到A8或A10。没有interhexamer氢键联系涉及A8在猪或牛胰岛素,身份的变化残留物似乎很少或根本没有影响六聚体的包装单元的细胞。相比之下,三个A10的侧链残留在一个三聚物使范德瓦耳斯接触A10侧链转化相关的六聚体。损失的C (delta1)原子的异亮氨酸残在猪生产胰岛素缬氨酸在牛胰岛素,0.36减少独立之间的距离对C(β)原子和一个0.24下降c尺寸的单位细胞。的影响在A10是序列的变化加强稳定疏水六聚体之间的相互作用。

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