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10.1074/jbc.RA117.001013 http://scihub22266oqcxt.onion/10.1074/jbc.RA117.001013 C5836122!5836122 !29317506     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29317506 &cmd=llinks): Failed to open stream: HTTP request failed! 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The interplay between citrullination and HLA-DRB1 polymorphism in shaping peptide binding hierarchies in rheumatoid arthritis |pdf=|usr=}}{{29317506 }} gab.com Text The interplay between citrullination and HLA-DRB1 polymorphism in shaping peptide binding hierarchies in rheumatoid arthritis JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=29317506 #FOAvip The HLA-DRB1 locus is strongly associated with rheumatoid arthritis (RA) susceptibility, whereupon citrullinated self-peptides bind to HLA-DR molecules bearing the shared epitope (SE) amino acid motif. However, the differing propensity for citrullinated/non-citrullinated self-peptides to bind given HLA-DR allomorphs remains unclear. Here, we used a fluorescence polarization assay to determine a hierarchy of binding affinities of 34 self-peptides implicated in RA against three HLA-DRB1 allomorphs (HLA-DRB1*04:01/*04:04/*04:05) each possessing the SE motif. For all three HLA-DRB1 allomorphs, we observed a strong correlation between binding affinity and citrullination at P4 of the bound peptide ligand. A differing hierarchy of peptide-binding affinities across the three HLA-DRB1 allomorphs was attributable to the ?-chain polymorphisms that resided outside the SE motif and were consistent with sequences of naturally presented peptide ligands. Structural determination of eight HLA-DR4-self-epitope complexes revealed strict conformational convergence of the P4-Cit and surrounding HLA ?-chain residues. Polymorphic residues that form part of the P1 and P9 pockets of the HLA-DR molecules provided a structural basis for the preferential binding of the citrullinated self-peptides to the HLA-DR4 allomorphs. Collectively, we provide a molecular basis for the interplay between citrullination of self-antigens and HLA polymorphisms that shape peptide-HLA-DR4 binding affinities in RA. Twit Text FOAVip The interplay between citrullination and HLA-DRB1 polymorphism in shaping peptide binding hierarchies in rheumatoid arthritis ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=29317506 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29317506 #FOAvip English Wikipedia <ref>{{Cite pmid|29317506 }}</ref> The interplay between citrullination and HLA-DRB1 polymorphism in shaping peptide binding hierarchies in rheumatoid arthritis #MMPMID29317506 Ting YT ; Petersen J ; Ramarathinam SH ; Scally SW ; Loh KL ; Thomas R ; Suri A ; Baker DG ; Purcell AW ; Reid HH ; Rossjohn J J Biol Chem 2018[Mar]; 293 (9 ): 3236-3251 PMID29317506 show ga The HLA-DRB1 locus is strongly associated with rheumatoid arthritis (RA) susceptibility, whereupon citrullinated self-peptides bind to HLA-DR molecules bearing the shared epitope (SE) amino acid motif. However, the differing propensity for citrullinated/non-citrullinated self-peptides to bind given HLA-DR allomorphs remains unclear. Here, we used a fluorescence polarization assay to determine a hierarchy of binding affinities of 34 self-peptides implicated in RA against three HLA-DRB1 allomorphs (HLA-DRB1*04:01/*04:04/*04:05) each possessing the SE motif. For all three HLA-DRB1 allomorphs, we observed a strong correlation between binding affinity and citrullination at P4 of the bound peptide ligand. A differing hierarchy of peptide-binding affinities across the three HLA-DRB1 allomorphs was attributable to the ?-chain polymorphisms that resided outside the SE motif and were consistent with sequences of naturally presented peptide ligands. Structural determination of eight HLA-DR4-self-epitope complexes revealed strict conformational convergence of the P4-Cit and surrounding HLA ?-chain residues. Polymorphic residues that form part of the P1 and P9 pockets of the HLA-DR molecules provided a structural basis for the preferential binding of the citrullinated self-peptides to the HLA-DR4 allomorphs. Collectively, we provide a molecular basis for the interplay between citrullination of self-antigens and HLA polymorphisms that shape peptide-HLA-DR4 binding affinities in RA. |*Citrullination [MESH] |*Polymorphism, Genetic [MESH] |Amino Acid Sequence [MESH] |Arthritis, Rheumatoid/*genetics/immunology/*metabolism [MESH] |Autoantigens/chemistry/metabolism [MESH] |Citrulline/metabolism [MESH] |HLA-DRB1 Chains/chemistry/*genetics/*metabolism [MESH] |Humans [MESH] |Models, Molecular [MESH] |Peptides/chemistry/*metabolism [MESH] |Protein Binding [MESH] |Protein Conformation, beta-Strand [MESH]The interplay between citrullination and HLA-DRB1 polymorphism in shap(epmc).pdf DeepDyve Pubget Overpricing