The inhibitory receptor LIR-1 uses a common binding interaction to recognize class I MHC molecules and the viral homolog UL18. (Q33883093)

29 July 2017

title

The inhibitory receptor LIR-1 uses a common binding interaction to recognize class I MHC molecules and the viral homolog UL18. (English)

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29 July 2017

Chapman TL

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29 July 2017

Heikeman AP

series ordinal

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29 July 2017

Bjorkman PJ

series ordinal

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29 July 2017

language of work or name

English

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publication date

1 November 1999

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29 July 2017

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29 July 2017

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29 July 2017

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29 July 2017

page(s)

603-613

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Human cytomegalovirus encodes a glycoprotein homologous to MHC class-I antigens

29 July 2017

cites work

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TAP- and tapasin-dependent HLA-E surface expression correlates with the binding of an MHC class I leader peptide

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A complex between the MHC class I homologue encoded by human cytomegalovirus and beta 2 microglobulin

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Characterization of a murine cytomegalovirus class I major histocompatibility complex (MHC) homolog: comparison to MHC molecules and to the human cytomegalovirus MHC homolog.

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Thermal stability comparison of purified empty and peptide-filled forms of a class I MHC molecule

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The MHC class I homolog encoded by human cytomegalovirus binds endogenous peptides

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Structure of the inhibitory receptor for human natural killer cells resembles haematopoietic receptors

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The MHC class I binding proteins LIR-1 and LIR-2 inhibit Fc receptor-mediated signaling in monocytes

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Modulation of natural killer cell cytotoxicity in human cytomegalovirus infection: the role of endogenous class I major histocompatibility complex and a viral class I homolog

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The ILT2(LIR1) and CD94/NKG2A NK cell receptors respectively recognize HLA-G1 and HLA-E molecules co-expressed on target cells

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The leukocyte Ig-like receptor (LIR)-1 for the cytomegalovirus UL18 protein displays a broad specificity for different HLA class I alleles: analysis of LIR-1 + NK cell clones

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Identifiers

DOI

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29 July 2017

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