Grueninger Dirk, Treiber Nora, Ziegler Mathias O P, Koetter Jochen W A, Schulze Monika-Sarah, Schulz Georg E
Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Albertstrasse 21, 79104 Freiburg im Breisgau, Germany.
Science. 2008 Jan 11;319(5860):206-9. doi: 10.1126/science.1150421.
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.
对蛋白质亚基之间以及蛋白质之间天然接触界面的分析揭示了一些支配它们缔合的一般规则。我们已应用这些规则来产生许多新型组装体，证明给定的蛋白质可以经过工程改造以在其表面的不同点形成接触。对称性起着重要作用，因为它定义了设计接触的多重性，从而决定了所需突变的数量。一些蛋白质仅需单个侧链改变就能缔合成高阶复合物。必须考虑埋藏侧链的流动性。已经对四个组装体进行了结构解析。设计的接触与结果之间的比较将为未来结构的开发提供有用的指导。
