| http://purl.uniprot.org/citations/30365927 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/30365927 | http://www.w3.org/2000/01/rdf-schema#comment | "X-ray crystallographic studies of class I peptide-MHC molecules (pMHC) continue to provide important insights into immune recognition, however their success depends on generation of diffraction-quality crystals, which remains a significant challenge. While protein engineering techniques such as surface-entropy reduction and lysine methylation have proven utility in facilitating and/or improving protein crystallisation, they risk affecting the conformation and biochemistry of the class I MHC antigen binding groove. An attractive alternative is the use of noncovalent crystallisation chaperones, however these have not been developed for pMHC. Here we describe a method for promoting class I pMHC crystallisation, by exploiting its natural ligand interaction with the immunoregulatory receptor LILRB1 as a novel crystallisation chaperone. First, focussing on a model HIV-1-derived HLA-A2-restricted peptide, we determined a 2.4 Å HLA-A2/LILRB1 structure, which validated that co-crystallisation with LILRB1 does not alter conformation of the antigenic peptide. We then demonstrated that addition of LILRB1 enhanced the crystallisation of multiple peptide-HLA-A2 complexes, and identified a generic condition for initial co-crystallisation. LILRB1 chaperone-based crystallisation enabled structure determination for HLA-A2 complexes previously intransigent to crystallisation, including both conventional and post-translationally-modified peptides, of diverse lengths. Since both the LILRB1 recognition interface on the HLA-A2 α3 domain molecule and HLA-A2-mediated crystal contacts are predominantly conserved across class I MHC molecules, the approach we outline could prove applicable to a diverse range of class I pMHC. LILRB1 chaperone-mediated crystallisation should expedite molecular insights into the immunobiology of diverse immune-related diseases and immunotherapeutic strategies, particularly involving class I pMHC complexes that are challenging to crystallise."xsd:string |
| http://purl.uniprot.org/citations/30365927 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jim.2018.10.011"xsd:string |
| http://purl.uniprot.org/citations/30365927 | http://purl.uniprot.org/core/author | "Mohammed F."xsd:string |
| http://purl.uniprot.org/citations/30365927 | http://purl.uniprot.org/core/author | "Willcox B.E."xsd:string |
| http://purl.uniprot.org/citations/30365927 | http://purl.uniprot.org/core/author | "Stones D.H."xsd:string |
| http://purl.uniprot.org/citations/30365927 | http://purl.uniprot.org/core/date | "2019"xsd:gYear |
| http://purl.uniprot.org/citations/30365927 | http://purl.uniprot.org/core/name | "J Immunol Methods"xsd:string |
| http://purl.uniprot.org/citations/30365927 | http://purl.uniprot.org/core/pages | "47-56"xsd:string |
| http://purl.uniprot.org/citations/30365927 | http://purl.uniprot.org/core/title | "Application of the immunoregulatory receptor LILRB1 as a crystallisation chaperone for human class I MHC complexes."xsd:string |
| http://purl.uniprot.org/citations/30365927 | http://purl.uniprot.org/core/volume | "464"xsd:string |
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