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Crystal structure of LIR-2 (ILT4) at 1.8 Å: differences from LIR-1 (ILT2) in regions implicated in the binding of the Human Cytomegalovirus class I MHC homolog UL18

11 Oct 2002

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PMID: 12390682
DOI: 10.1186/1472-6807-2-6

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Crystal structure of LIR-2 (ILT4) at 1.8 Å: differences from LIR-1 (ILT2) in regions implicated in the binding of the Human Cytomegalovirus class I MHC homolog UL18PMID 12390682Read ↗

Crystal structure of HLA-A2 bound to LIR-1, a host and viral major histocompatibility complex receptorSemantic proximity Read ↗

Structure of UL18, a peptide-binding viral MHC mimic, bound to a host inhibitory receptorSemantic proximity Read ↗

Application of the immunoregulatory receptor LILRB1 as a novel crystallisation chaperone for class I peptide-MHC complexesSemantic proximity Read ↗

The inhibitory receptor LIR-1 uses a common binding interaction to recognize class I MHC molecules and the viral homolog UL18.Semantic proximity Read ↗

The structure of cytomegalovirus immune modulator UL141 highlights structural Ig-fold versatility for receptor binding.Semantic proximity Read ↗

Genetic variability of the major histocompatibility complex class I homologue encoded by human cytomegalovirus leads to differential binding to the inhibitory receptor ILT2.Semantic proximity Read ↗

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Crystal structure of human cytomegalovirus IL-10 bound to soluble human IL-10R1Semantic proximity Read ↗

Insights into the binding recognition and computational design of IL-2 muteins with enhanced predicted binding affinity to the IL-2 receptor α.Semantic proximity Read ↗

Crystal structure of extracellular domain of human lectin-like transcript 1 (LLT1), the ligand for natural killer receptor-P1A.Semantic proximity Read ↗

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