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Structural basis of mouse cytomegalovirus m152/gp40 interaction with RAE1γ reveals a paradigm for MHC/MHC interaction in immune evasion.
Kannan Natarajan, Elliott Margulies, Howard Robinson, Rui Wang, Li Zhi-Heng, Norman Boyd, Maria Jamela R Revilleza, Huaying Zhao
2012-12-18
Animals, Drosophila, metabolism, Escherichia coli, Gene Expression Regulation, Viral, HEK293 Cells, Humans, Immune System, Killer Cells, Natural, Ligands, Major Histocompatibility Complex, immunology, Membrane Glycoproteins, Mice, Molecular Conformation, Muromegalovirus, Mutation, NK Cell Lectin-Like Receptor Subfamily K, chemistry, Nuclear Matrix-Associated Proteins, Nucleocytoplasmic Transport Proteins, Protein Conformation, Protein Isoforms, Protein Structure, Secondary, Surface Plasmon Resonance, Viral Proteins, X-Ray Diffraction
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Animals,Drosophila,metabolism,Escherichia coli,Gene Expression Regulation, Viral,HEK293 Cells,Humans,Immune System,Killer Cells, Natural,Ligands,Major Histocompatibility Complex,immunology,Membrane Glycoproteins,Mice,Molecular Conformation,Muromegalovirus,Mutation,NK Cell Lectin-Like Receptor Subfamily K,chemistry,Nuclear Matrix-Associated Proteins,Nucleocytoplasmic Transport Proteins,Protein Conformation,Protein Isoforms,Protein Structure, Secondary,Surface Plasmon Resonance,Viral Proteins,X-Ray Diffraction
Animals, Drosophila, metabolism, Escherichia coli, Gene Expression Regulation, Viral, HEK293 Cells, Humans, Immune System, Killer Cells, Natural, Ligands, Major Histocompatibility Complex, immunology, Membrane Glycoproteins, Mice, Molecular Conformation, Muromegalovirus, Mutation, NK Cell Lectin-Like Receptor Subfamily K, chemistry, Nuclear Matrix-Associated Proteins, Nucleocytoplasmic Transport Proteins, Protein Conformation, Protein Isoforms, Protein Structure, Secondary, Surface Plasmon Resonance, Viral Proteins, X-Ray Diffraction