Center for Computational Biology and Bioinformatics, College of Engineering, Koc University, Istanbul, Turkey.
Protein Eng Des Sel. 2011 Sep;24(9):635-48. doi: 10.1093/protein/gzr025. Epub 2011 Jun 15.
Transient complexes are crucial for diverse biological processes such as biochemical pathways and signaling cascades in the cell. Here, we give an overview of the transient interactions; the importance of transient interactions as drug targets; and the structural characterization of transient protein-protein complexes based on the geometrical and physicochemical features of the transient complexes' interfaces. To better understand and eventually design transient protein-protein interactions (TPPIs), a molecular perspective of the protein-protein interfaces is necessary. Obtaining high-quality structures of protein-protein interactions could be one way of achieving this goal. After introducing the association kinetics of TPPIs, we elaborate on the experimental techniques detecting TPPIs in combination with the computational methods which classify transient and/or non-obligate complexes. In this review, currently available databases and servers that can be used to identify and predict TPPIs are also compiled.
瞬态复合物对于多种生物过程至关重要,如细胞内的生化途径和信号级联。在这里,我们概述了瞬态相互作用;瞬态相互作用作为药物靶点的重要性;以及基于瞬态复合物界面的几何和物理化学特征对瞬态蛋白-蛋白复合物的结构特征。为了更好地理解并最终设计瞬态蛋白-蛋白相互作用(TPPIs),有必要从分子角度研究蛋白-蛋白界面。获得高质量的蛋白-蛋白相互作用结构可能是实现这一目标的一种方法。在介绍 TPPIs 的缔合动力学之后,我们详细阐述了检测 TPPIs 的实验技术,并结合分类瞬态和/或非必需复合物的计算方法。在这篇综述中,还编译了目前可用于识别和预测 TPPIs 的数据库和服务器。