4ll9 | pdb_00004ll9

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Template:STRUCTURE 4ll9

Crystal structure of D3D4 domain of the LILRB1 molecule

Template:ABSTRACT PUBMED 23955630

Function

[LIRB1_HUMAN] Receptor for class I MHC antigens. Recognizes a broad spectrum of HLA-A, HLA-B, HLA-C and HLA-G alleles. Receptor for H301/UL18, a human cytomegalovirus class I MHC homolog. Ligand binding results in inhibitory signals and down-regulation of the immune response. Engagement of LILRB1 present on natural killer cells or T-cells by class I MHC molecules protects the target cells from lysis. Interaction with HLA-B or HLA-E leads to inhibition of the signal triggered by FCER1A and inhibits serotonin release. Inhibits FCGR1A-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions.[1] [2] [3]

About this Structure

4ll9 is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  1. Nam G, Shi Y, Ryu M, Wang Q, Song H, Liu J, Yan J, Qi J, Gao GF. Crystal structures of the two membrane-proximal Ig-like domains (D3D4) of LILRB1/B2: alternative models for their involvement in peptide-HLA binding. Protein Cell. 2013 Aug 17. PMID:23955630 doi:10.1007/s13238-013-3908-x
  1. ↑ Cosman D, Fanger N, Borges L, Kubin M, Chin W, Peterson L, Hsu ML. A novel immunoglobulin superfamily receptor for cellular and viral MHC class I molecules. Immunity. 1997 Aug;7(2):273-82. PMID:9285411
  2. ↑ Fanger NA, Cosman D, Peterson L, Braddy SC, Maliszewski CR, Borges L. The MHC class I binding proteins LIR-1 and LIR-2 inhibit Fc receptor-mediated signaling in monocytes. Eur J Immunol. 1998 Nov;28(11):3423-34. PMID:9842885
  3. ↑ Bellon T, Kitzig F, Sayos J, Lopez-Botet M. Mutational analysis of immunoreceptor tyrosine-based inhibition motifs of the Ig-like transcript 2 (CD85j) leukocyte receptor. J Immunol. 2002 Apr 1;168(7):3351-9. PMID:11907092

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