A conserved trimerization motif controls the topology of short coiled coils
A conserved trimerization motif controls the topology of short coiled coils
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DOI：
10.1073/pnas.0502390102
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发表时间：
2005-09-27
影响因子：
11.1
通讯作者：
Steinmetz, MO
中科院分区：
文献类型：
--
作者：
Kammerer, RA;Kostrewa, D;Steinmetz, MO
近年来，短螺旋线圈已被用于从生物材料到医学科学的应用范围。对于这些应用中的许多应用，控制工程蛋白质系统的拓扑结构的因素的知识是必不可少的。在这里，我们证明了短卷曲螺旋的三聚化是由一个独特的结构基序决定的，该结构基序包括表面盐桥的特定网络和最佳的疏水性包装相互作用。该基序在细胞内、细胞外、病毒和合成蛋白中是保守的，并且定义了短卷曲螺旋的三聚体形成的通用分子决定簇。除了对候选治疗蛋白的生物技术生产特别感兴趣之外，这些发现可能对病毒药物开发策略感兴趣。
In recent years, short coiled coils have been used for applications ranging from biomaterial to medical sciences. For many of these applications knowledge of the factors that control the topology of the engineered protein systems is essential. Here, we demonstrate that trimerization of short coiled coils is determined by a distinct structural motif that encompasses specific networks of surface salt bridges and optimal hydrophobic packing interactions. The motif is conserved among intracellular, extracellular, viral, and synthetic proteins and defines a universal molecular determinant for trimer formation of short coiled coils. In addition to being of particular interest for the biotechnological production of candidate therapeutic proteins, these findings may be of interest for viral drug development strategies.