| http://purl.uniprot.org/citations/32424043 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/32424043 | http://www.w3.org/2000/01/rdf-schema#comment | "Human leukocyte immunoglobulin-like receptors (LILRs) typically regulate immune activation by binding to the human leukocyte antigen class I molecules. LILRA2, a member of the LILR family, was recently reported to bind to other unique ligands, the bacterially degraded Igs (N-truncated Igs), for the activation of immune cells. Therefore, LILRA2 is currently attracting significant attention as a novel innate immune receptor. However, the detailed recognition mechanisms required for this interaction remain unclear. In this study, using several biophysical techniques, we uncovered the molecular mechanism of N-truncated Ig recognition by LILRA2. Surface plasmon resonance analysis disclosed that LILRA2 specifically binds to N-truncated Ig with weak affinity (Kd = 4.8 μm) and fast kinetics. However, immobilized LILRA2 exhibited a significantly enhanced interaction with N-truncated Ig due to avidity effects. This suggests that cell surface-bound LILRA2 rapidly monitors and identifies bi- or multivalent abnormal N-truncated Igs through specific cross-linking to induce immune activation. Van't Hoff analysis revealed that this interaction is enthalpy-driven, with a small entropy loss, and results from differential scanning calorimetry indicated the instability of the putative LILRA2-binding site, the Fab region of the N-truncated Ig. Atomic force microscopy revealed that N truncation does not cause significant structural changes in Ig. Furthermore, mutagenesis analysis identified the hydrophobic region of LILRA2 domain 2 as the N-truncated Ig-binding site, representing a novel ligand-binding site for the LILR family. These results provide detailed insights into the molecular regulation of LILR-mediated immune responses targeting ligands that have been modified by bacteria."xsd:string |
| http://purl.uniprot.org/citations/32424043 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.ra120.013354"xsd:string |
| http://purl.uniprot.org/citations/32424043 | http://purl.uniprot.org/core/author | "Maenaka K."xsd:string |
| http://purl.uniprot.org/citations/32424043 | http://purl.uniprot.org/core/author | "Yamazaki R."xsd:string |
| http://purl.uniprot.org/citations/32424043 | http://purl.uniprot.org/core/author | "Fukuhara H."xsd:string |
| http://purl.uniprot.org/citations/32424043 | http://purl.uniprot.org/core/author | "Furukawa A."xsd:string |
| http://purl.uniprot.org/citations/32424043 | http://purl.uniprot.org/core/author | "Arase H."xsd:string |
| http://purl.uniprot.org/citations/32424043 | http://purl.uniprot.org/core/author | "Hirayasu K."xsd:string |
| http://purl.uniprot.org/citations/32424043 | http://purl.uniprot.org/core/author | "Yumoto K."xsd:string |
| http://purl.uniprot.org/citations/32424043 | http://purl.uniprot.org/core/date | "2020"xsd:gYear |
| http://purl.uniprot.org/citations/32424043 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/32424043 | http://purl.uniprot.org/core/pages | "9531-9541"xsd:string |
| http://purl.uniprot.org/citations/32424043 | http://purl.uniprot.org/core/title | "Molecular mechanism of the recognition of bacterially cleaved immunoglobulin by the immune regulatory receptor LILRA2."xsd:string |
| http://purl.uniprot.org/citations/32424043 | http://purl.uniprot.org/core/volume | "295"xsd:string |
| http://purl.uniprot.org/citations/32424043 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/32424043 |
| http://purl.uniprot.org/citations/32424043 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/32424043 |
| http://purl.uniprot.org/uniprot/#_A0A0D9SFC7-mappedCitation-32424043 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/32424043 |
| http://purl.uniprot.org/uniprot/#_A0A0G2JMC9-mappedCitation-32424043 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/32424043 |
| http://purl.uniprot.org/uniprot/#_A0A0G2JMW8-mappedCitation-32424043 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/32424043 |
| http://purl.uniprot.org/uniprot/#_A8MZH0-mappedCitation-32424043 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/32424043 |
| http://purl.uniprot.org/uniprot/#_Q8N149-mappedCitation-32424043 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/32424043 |
| http://purl.uniprot.org/uniprot/#_Q99702-mappedCitation-32424043 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/32424043 |
| http://purl.uniprot.org/uniprot/Q8N149 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/32424043 |
| http://purl.uniprot.org/uniprot/A8MZH0 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/32424043 |