Evolutionary conservation in multiple faces of protein interaction
BackgroundProtein interfaces are believed to be evolutionarily more conserved than the rest of the protein surface, but this has not been properly verified using a large protein structural set. Furthermore, recent systematic protein interaction analyses have proved that hub proteins, interacting with many partners, have multiple interfaces to connect protein interaction networks, which have never taken into account for conservation analysis of protein interface. Here, we studied the evolutionary conservation of protein interfaces using a large-scale dataset of 3,844protein complexes and all their known multiple interfaces. We found that protein interfaces were indeed more conserved than non-interface surfaces, and the conservation level of protein interfaces increased when multiple interfaces were properly considered. These findings suggest that conservation analysis should be a good descriptor for protein interface identification and proteinprotein interaction predictions. We applied this evolutionary feature to filter docking decoys and found that protein interface conservation worked remarkably well in selecting the near-native structures from the large number of generated docking complexes.Finally, our results reveal new aspects of protein interface evolution, which explain the correlation within interface conservation, the number of interfaces, and the size of interfaces.
Yoon Sup Choi Jae-Seong Yang Sung Ho Ryu Sanguk Kim
School of Interdisciplinary Bioscience and Bioengineering, Pohang University of Science and Technolo School of Interdisciplinary Bioscience and Bioengineering, Pohang University of Science and Technolo
国际会议
The 7th Asia-Pacific Bioinformatics Conference(第七届亚太生物信息学大会)
北京
英文
869
2009-01-01（万方平台首次上网日期，不代表论文的发表时间）