7DC6
Giant panda MHC class I complexes
Summary for 7DC6
Entry DOI | 10.2210/pdb7dc6/pdb |
Descriptor | MHC class I antigen, Beta-2-microglobulin, CCV-NGY9 peptide from Spike protein, ... (4 entities in total) |
Functional Keywords | giant panda, mhc class i, aime-128, immune system |
Biological source | Ailuropoda melanoleuca (Giant panda) More |
Total number of polymer chains | 6 |
Total formula weight | 88902.07 |
Authors | |
Primary citation | Yuan, H.,Ma, L.,Zhang, L.,Li, X.,Xia, C. Crystal structure of the giant panda MHC class I complex: First insights into the viral peptide presentation profile in the bear family. Protein Sci., 29:2468-2481, 2020 Cited by PubMed Abstract: The viral cytotoxic T lymphocyte (CTL) epitope peptides presented by classical MHC-I molecules require the assembly of a peptide-MHC-I-β2m (pMHC-I) trimolecular complex for T cell receptor (TCR) recognition, which is the critical activation link for triggering antiviral T cell immunity. Research on T cell immunology in the Ursidae family, especially structural immunology, is still lacking. In this study, the structure of the key trimolecular complex pMHC-I, which binds a peptide from canine distemper virus, was solved for the first time using giant panda as a representative species of Ursidae. The structural characteristics of the giant panda pMHC-I complex (pAime-128), including the unique pockets in the peptide-binding groove (PBG), were analyzed in detail. Comparing the pAime-128 to others in the bear family and extending the comparison to other mammals revealed distinct features. The interaction between MHC-I and β2m, the features of pAime-128 involved in TCR docking and cluster of differentiation 8 (CD8) binding, the anchor sites in the PBG, and the CTL epitopes of potential viruses that infect pandas were clarified. Unique features of pMHC-I viral antigen presentation in the panda were revealed by solving the three-dimensional (3D) structure of pAime-128. The distinct characteristics of pAime-128 indicate an unusual event that emerged during the evolution of the MHC system in the bear family. These results provide a new platform for research on panda CTL immunity and the design of vaccines for application in the bear family. PubMed: 33078460DOI: 10.1002/pro.3980 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.68 Å) |
Structure validation
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