3Q2C

Binding properties to HLA class I molecules and the structure of the leukocyte Ig-like receptor A3 (LILRA3/ILT6/LIR4/CD85e)

3Q2C の概要

• エントリーDOI: 10.2210/pdb3q2c/pdb
• 関連するPDBエントリー: 1VDG
• 分子名称: Leukocyte immunoglobulin-like receptor subfamily A member 3 (2 entities in total)
• 機能のキーワード: lilra3, ilt6, activating receptor, hla binding, immune system
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10792.34

構造登録者

Ryu, M.,Chen, Y.,Qi, J.X.,Liu, J.,Shi, Y.,Cheng, H.,Gao, G.F. (登録日: 2010-12-20, 公開日: 2011-07-13, 最終更新日: 2024-10-30)

主引用文献

Ryu, M.,Chen, Y.,Qi, J.,Liu, J.,Fan, Z.,Nam, G.,Shi, Y.,Cheng, H.,Gao, G.F.
LILRA3 binds both classical and non-classical HLA class I molecules but with reduced affinities compared to LILRB1/LILRB2: structural evidence
Plos One, 6:e19245-e19245, 2011

PubMed Abstract: Structurally, Group 1 LILR (Leukocyte Immunoglobulin (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.

PubMed: 21559424
DOI: 10.1371/journal.pone.0019245

実験手法

X-RAY DIFFRACTION (2.5 Å)