Designed protein-protein association
Designed protein-protein association
复制标题
DOI：
10.1126/science.1150421
复制
发表时间：
2008-01-11
期刊：
影响因子：
56.9
通讯作者：
Schulz, Georg E.
中科院分区：
文献类型：
--
作者：
Grueninger, Dirk;Treiber, Nora;Schulz, Georg E.
对蛋白质亚基之间和蛋白质之间的自然接触界面的分析揭示了一些支配它们之间联系的一般规则。我们已经应用这些规则生产了许多新的组件，证明了给定的蛋白质可以被设计成在其表面的不同点形成接触。对称性扮演着重要的角色，因为它定义了设计接触的多重性，从而定义了所需突变的数量。其中一些蛋白质只需要一个侧链的改变就可以与更高阶的复合体结合。必须考虑埋在地下的侧链的流动性。已经从结构上阐明了四个组装体。将设计的触点与结果进行比较，将为未来架构的开发提供有用的指导。
The analysis of natural contact interfaces between protein subunits and between proteins has disclosed some general rules governing their association. We have applied these rules to produce a number of novel assemblies, demonstrating that a given protein can be engineered to form contacts at various points of its surface. Symmetry plays an important role because it defines the multiplicity of a designed contact and therefore the number of required mutations. Some of the proteins needed only a single side- chain alteration in order to associate to a higher- order complex. The mobility of the buried side chains has to be taken into account. Four assemblies have been structurally elucidated. Comparisons between the designed contacts and the results will provide useful guidelines for the development of future architectures.