2D3V
Crystal Structure of Leukocyte Ig-like Receptor A5 (LILRA5/LIR9/ILT11)
Summary for 2D3V
| Entry DOI | 10.2210/pdb2d3v/pdb |
| Descriptor | leukocyte immunoglobulin-like receptor subfamily A member 5 isoform 1 (2 entities in total) |
| Functional Keywords | immunoglobulin-like fold, immune system |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 22123.56 |
| Authors | Shiroishi, M.,Kajikawa, M.,Kuroki, K.,Ose, T.,Kohda, D.,Maenaka, K. (deposition date: 2005-10-03, release date: 2006-06-06, Last modification date: 2024-10-30) |
| Primary citation | Shiroishi, M.,Kajikawa, M.,Kuroki, K.,Ose, T.,Kohda, D.,Maenaka, K. Crystal structure of the human monocyte-activating receptor, J.Biol.Chem., 281:19536-19544, 2006 Cited by PubMed Abstract: Human leukocyte Ig-like receptor B1 (LILRB1) and B2 (LILRB2) belong to "Group 1" receptors and recognize a broad range of major histocompatibility complex class I molecules (MHCIs). In contrast, "Group 2" receptors show low similarity with LILRB1/B2, and their ligands remain to be identified. To date, the structural and functional characteristics of Group 2 LILRs are poorly understood. Here we report the crystal structure of the extracellular domain of LILRA5, which is an activating Group 2 LILR expressed on monocytes and neutrophils. Unexpectedly, the structure showed large changes in structural conformation and charge distribution in the region corresponding to the MHCI binding site of LILRB1/B2, which are also distinct from killer cell Ig-like receptors and Fc alpha receptors. These changes probably confer the structural hindrance for the MHCI binding, and their key amino acid substitutions are well conserved in Group 2 LILRs. Consistently, the surface plasmon resonance and flow cytometric analyses demonstrated that LILRA5 exhibited no affinities to all tested MHCIs. These results raised the possibility that LILRA5 as well as Group 2 LILRs do not play a role in any MHCI recognition but could possibly bind to non-MHCI ligand(s) on the target cells to provide a novel immune regulation mechanism. PubMed: 16675463DOI: 10.1074/jbc.M603076200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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