Han Jung-Hoon, Batey Sarah, Nickson Adrian A, Teichmann Sarah A, Clarke Jane
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
Nat Rev Mol Cell Biol. 2007 Apr;8(4):319-30. doi: 10.1038/nrm2144. Epub 2007 Mar 14.
Analyses of genomes show that more than 70% of eukaryotic proteins are composed of multiple domains. However, most studies of protein folding focus on individual domains and do not consider how interactions between domains might affect folding. Here, we address this by analysing the three-dimensional structures of multidomain proteins that have been characterized experimentally and observe that where the interface is small and loosely packed, or unstructured, the folding of the domains is independent. Furthermore, recent studies indicate that multidomain proteins have evolved mechanisms to minimize the problems of interdomain misfolding.
基因组分析表明，超过70%的真核生物蛋白质由多个结构域组成。然而，大多数蛋白质折叠研究集中在单个结构域上，并未考虑结构域之间的相互作用如何影响折叠。在此，我们通过分析已通过实验表征的多结构域蛋白质的三维结构来解决这一问题，并观察到当界面较小且堆积松散或无结构时，结构域的折叠是独立的。此外，最近的研究表明，多结构域蛋白质已经进化出机制来最小化结构域间错误折叠的问题。
