The structural basis of chicken, swine and bovine CD8 alpha alpha dimers provides insight into the co-evolution with MHC I in endotherm species

文献类型： 外文期刊

第一作者： Liu, Yanjie

作者： Liu, Yanjie;Li, Xin;Zhang, Nianzhi;Xia, Chun;Liu, Yanjie;Qi, Jianxun;Xia, Chun

作者机构：

期刊名称：SCIENTIFIC REPORTS （ 影响因子：4.379； 五年影响因子：5.133 ）

ISSN： 2045-2322

年卷期： 2016 年 6 卷

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收录情况： SCI

摘要： It is unclear how the pivotal molecules of the adaptive immune system (AIS) maintain their inherent characteristics and relationships with their co-receptors over the course of co-evolution. CD8 alpha, a fundamental but simple AIS component with only one immunoglobulin variable (IgV) domain, is a good example with which to explore this question because it can fold correctly to form homodimers (CD8 alpha alpha) and interact with peptide-MHC I (p/MHC I) with low sequence identities between different species. Hereby, we resolved the crystal structures of chicken, swine and bovine CD8 alpha alpha. They are typical homodimers consisting of two symmetric IgV domains with distinct species specificities. The CD8 alpha alpha structures indicated that a few highly conserved residues are important in CD8 dimerization and in interacting with p/MHC I. The dimerization of CD8 alpha alpha mainly depends on the pivotal residues on the dimer interface; in particular, four aromatic residues provide many intermolecular forces and contact areas. Three residues on the surface of CD8 alpha connecting cavities that formed most of the hydrogen bonds with p/MHC I were also completely conserved. Our data propose that a few key conserved residues are able to ensure the CD8 alpha own structural characteristics despite the great sequence variation that occurs during evolution in endotherms.

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