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- W1999839845 abstract "Lysis of target cells by natural killer (NK) cells can be prevented by killer cell inhibitory receptors (KIR) specific for major histocompatibility complex class I molecules. Functional studies have identified two distinct p58 KIR, each reactive with a different group of HLA-C allotypes, and distinct p70 KIR specific for some HLA-B or HLA-A allotypes. The NK specificities for each group of HLA-C allotypes have been reproduced by direct binding of recombinant soluble p58 molecules. Here, we show that a soluble p70 KIR binds to HLA-B*5101, but not to HLA-A or HLA-C molecules. Truncated soluble forms of the HLA-B*5101-specific p70 KIR, including one with two immunoglobulin (Ig) domains reactive with a monoclonal antibody that blocks p70 KIR function, did not bind to HLA-B*5101, indicating that all three Ig domains are required for binding." @default.
- W1999839845 created "2016-06-24" @default.
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- W1999839845 date "1997-02-01" @default.
- W1999839845 modified "2023-09-28" @default.
- W1999839845 title "Binding of a soluble p70 killer cell inhibitory receptor to HLA-B*5101: Requirement for all three p70 immunoglobulin domains" @default.
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- W1999839845 doi "https://doi.org/10.1002/eji.1830270231" @default.
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