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作 者:SONG Zhe LIU Tao JIAO ChunBo LIU Wei ZHU MingHua GUO YangFan WANG XiaoGang
机构地区:[1]College of Advanced Science and Technology,Dalian University of Technology,Dalian 116024,China [2]Department of Physics,Dalian University of Technology,Dalian 116024,China
出 处:《Science China Chemistry》2009年第1期39-47,共9页中国科学(化学英文版)
摘 要:In the MHC class I molecule binding antigenic peptides processing and presentation pathway, the ubiquitin-proteasome system plays a key role in degrading the protein substrate. For the purpose of studying the specificities of proteasomal cleavage sites, partial least squares method is used to predict the proteasomal cleavage sites, and the predictive accuracy of the model is 82.8%. The specificities of the cleavage sites and the adjacent positions come from the contribution of the amino acids of the samples to the cleavage sites, showing the information of proteasome interacting with antigen protein. It demonstrates that the proteasome cleaving to target protein is selective, but not random.In the MHC classⅠmolecule binding antigenic peptides processing and presentation pathway,the ubiquitin-proteasome system plays a key role in degrading the protein substrate.For the purpose of studying the specificities of proteasomal cleavage sites,partial least squares method is used to predict the proteasomal cleavage sites,and the predictive accuracy of the model is 82.8%.The specificities of the cleavage sites and the adjacent positions come from the contribution of the amino acids of the samples to the cleavage sites,showing the information of proteasome interacting with antigen protein.It demonstrates that the proteasome cleaving to target protein is selective,but not random.
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