Functional determinants of protein assembly into homomeric complexes.-猫眼课题宝

DOI：

10.1038/s41598-017-05084-8

发表时间：

2017-07-10

期刊：

Scientific reports

影响因子：

4.6

通讯作者：

中科院分区：

综合性期刊3区

文献类型：

作者：

Bergendahl LT;Marsh JA

来源链接：

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5504011/

Approximately half of proteins with experimentally determined structures can interact with other copies of themselves and assemble into homomeric complexes, the overwhelming majority of which (>96%) are symmetric. Although homomerisation is often assumed to a functionally beneficial result of evolutionary selection, there has been little systematic analysis of the relationship between homomer structure and function. Here, utilizing the large numbers of structures and functional annotations now available, we have investigated how proteins that assemble into different types of homomers are associated with different biological functions. We observe that homomers from different symmetry groups are significantly enriched in distinct functions, and can often provide simple physical and geometrical explanations for these associations in regards to substrate recognition or physical environment. One of the strongest associations is the tendency for metabolic enzymes to form dihedral complexes, which we suggest is closely related to allosteric regulation. We provide a physical explanation for why allostery is related to dihedral complexes: it allows for efficient propagation of conformational changes across isologous (i.e. symmetric) interfaces. Overall we demonstrate a clear relationship between protein function and homomer symmetry that has important implications for understanding protein evolution, as well as for predicting protein function and quaternary structure.