Structural insights into the backbone-circularized granulocyte colony-stimulating factor containing a short connector
Structural insights into the backbone-circularized granulocyte colony-stimulating factor containing a short connector
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DOI：
10.1016/j.bbrc.2018.04.045
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发表时间：
2018-06-02
影响因子：
3.1
通讯作者：
Honda, Shinya
中科院分区：
文献类型：
--
作者：
Miyafusa, Takamitsu;Shibuya, Risa;Honda, Shinya
骨架环化是增强多肽结构稳定性的有效方法。在这里，我们提出了环化的粒细胞集落刺激因子（G-CSF）的变体的晶体结构，其中的末端螺旋区域使用短的，两个氨基酸的连接器环化。结构显示N-和C-末端确实通过肽键连接。C-末端区域的局部结构从a螺旋过渡到310螺旋，靠近N-末端区域有一个弯曲，表明结构变化抵消了连接器的不足长度。这是有史以来第一次报道环状蛋白质骨架的晶体结构。它将促进骨干循环化方法的发展。(C)2018爱思唯尔公司All rights reserved.
Backbone circularization is a powerful approach for enhancing the structural stability of polypeptides. Herein, we present the crystal structure of the circularized variant of the granulocyte colony-stimulating factor (G-CSF) in which the terminal helical region was circularized using a short, two-amino acid connector. The structure revealed that the N- and C-termini were indeed connected by a peptide bond. The local structure of the C-terminal region transited from an a helix to 310 helix with a bend close to the N-terminal region, indicating that the structural change offset the insufficient length of the connector. This is the first-ever report of a crystal structure of the backbone of a circularized protein. It will facilitate the development of backbone circularization methodology. (C) 2018 Elsevier Inc. All rights reserved.