id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-013894-1bgvj62a	Wang, Qihui	Structures of the four Ig-like domain LILRB2 and the four-domain LILRB1 and HLA-G1 complex	2019-07-04		.txt	text/plain	6883	408	65	Through cis or trans interactions with human leukocyte antigen (HLA)-G, the two most abundantly expressed inhibitory LILRs, LILRB1, and LILRB2 (LILRB1/2, also known as CD85j/d and ILT2/4), are involved in immunotolerance in pregnancy and transplantation, autoimmune diseases, and immune evasion by tumors. Structural comparisons of LILRB1/2 binding to different HLA alleles Similar to previous reports, 14,17 D1 interacts with the HLA-G1 α3 domain. As assessed by the SPR assay, dimeric HLA-G1 presenting variable peptides displayed similar binding strengths for LILRB1 and LILRB2 (with four Ig-like domains or D1D2), indicating that the peptides seem to have no effect on the interactions. Structural data in this study indicate that through trans interaction, one HLA-G1 monomer binds to one LILRB1/2 molecule. The complex structure reported here provides the first direct evidence that D1D2 is responsible for all of the interactions with HLA-Is, while D3D4 is not the reason to explain why HLA-Is that carry a single residue substitution in their α1α2 domains or in the presented peptides display variable binding affinities to LILRB2.	./cache/cord-013894-1bgvj62a.txt	./txt/cord-013894-1bgvj62a.txt