Centre for Medical Research, The University of Western Australia, Nedlands, WA.
Cell Stress Chaperones. 2011 Jul;16(4):353-67. doi: 10.1007/s12192-010-0248-0. Epub 2010 Dec 9.
The tetratricopeptide repeat (TPR) motif is one of many repeat motifs that form structural domains in proteins that can act as interaction scaffolds in the formation of multi-protein complexes involved in numerous cellular processes such as transcription, the cell cycle, protein translocation, protein degradation and host defence against invading pathogens. The crystal structures of many TPR domain-containing proteins have been determined, showing TPR motifs as two anti-parallel α-helices packed in tandem arrays to form a structure with an amphipathic groove which can bind a target peptide. This is however not the only mode of target recognition by TPR domains, with short amino acid insertions and alternative TPR motif conformations also shown to contribute to protein interactions, highlighting diversity in TPR domains and the versatility of this structure in mediating biological events.
四肽重复（TPR）基序是许多重复基序之一，这些基序形成蛋白质中的结构域，可作为参与众多细胞过程（如转录、细胞周期、蛋白质易位、蛋白质降解和宿主防御入侵病原体）的多蛋白复合物形成的相互作用支架。许多包含 TPR 结构域的蛋白质的晶体结构已经确定，显示 TPR 基序作为两个反平行的α-螺旋串联排列，形成具有两亲性沟槽的结构，可结合靶肽。然而，这并不是 TPR 结构域识别靶标的唯一模式，短氨基酸插入和替代 TPR 基序构象也被证明有助于蛋白质相互作用，突出了 TPR 结构域的多样性和这种结构在介导生物学事件中的多功能性。
