3Q2C
Binding properties to HLA class I molecules and the structure of the leukocyte Ig-like receptor A3 (LILRA3/ILT6/LIR4/CD85e)
Summary for 3Q2C
| Entry DOI | 10.2210/pdb3q2c/pdb |
| Related | 1VDG |
| Descriptor | Leukocyte immunoglobulin-like receptor subfamily A member 3 (2 entities in total) |
| Functional Keywords | lilra3, ilt6, activating receptor, hla binding, immune system |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 10792.34 |
| Authors | |
| Primary citation | 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 Cited by 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: 21559424DOI: 10.1371/journal.pone.0019245 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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