LILRA3 binds both classical and non-classical HLA class I molecules but with reduced affinities compared to LILRB1/LILRB2: structural evidence.

LILRA3 binds both classical and non-classical HLA class I molecules but with reduced affinities compared to LILRB1/LILRB2: structural evidence.
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DOI:
10.1371/journal.pone.0019245
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发表时间:
2011-04-29
期刊:
影响因子:
3.7
通讯作者:
Gao GF
Gao GF
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Ryu M;Chen Y;Qi J;Liu J;Fan Z;Nam G;Shi Y;Cheng H;Gao GF

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在结构上,第1组LILR(白细胞免疫球蛋白(Ig)样受体,也称为Ig样转录物,ILT;白细胞igg样受体;和CD85)成员在HLAIs(人类白细胞抗原I类分子)结合区域方面非常相似,并且假设它们都与HLAIs结合。作为第1组LILR之一,LILRA3是唯一的分泌型LILR,可以极大地控制LILRB1、LILRB2以及LILRA1等与hla结合的LILR分子诱导的抑制性免疫反应。然而,对于LILRA3与hla的结合知之甚少。在本报告中,我们展示了LILRA3结构域1 (D1)的晶体结构,并利用BIAcore®表面等离子体共振分析(SPR)评估了D1和D1D2(结构域1和结构域2)与经典和非经典hla的结合。我们发现LILRA3结合经典HLA-A*0201和非经典HLA-G1,但与LILRB1或LILRB2相比,其亲和力降低。多态氨基酸和lilra3d1结构支持这一观点。
Structurally, Group 1 LILR (Leukocyte Immunogloblin (Ig)-Like Receptor, also known as Ig-like transcripts, ILT; Leukocyte Ig-like receptor, LIR; and CD85) members are very similar in terms of the HLAIs (human leukocyte antigen class I molecules) binding region and were hypothesized that they all bind to HLAIs. As one of the Group 1 LILRs, LILRA3 is the only secretory LILR and may greatly control the inhibitory immune response induced by LILRB1, LILRB2, and other HLA-binding LILR molecules like LILRA1. Nevertheless, little was known about the binding of LILRA3 to HLAIs. In this report, we present the crystal structure of the LILRA3 domain 1 (D1) and evaluate the D1 and D1D2 (domain 1 and domain 2) binding to classical and non-classical HLAIs using BIAcore® surface plasmon resonance analysis (SPR). We found that LILRA3 binds both classical HLA-A*0201 and non-classical HLA-G1 but with reduced affinities compared to either LILRB1 or LILRB2. The polymorphic amino acids and the LILRA3 D1 structure support this notion.
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