6YXM6YXM の概要
| エントリーDOI | 10.2210/pdb6yxm/pdb |
| 分子名称 | CII-C-39-CIT, ACPA 1F2 Fab fragment - heavy chain, ACPA 1F2 Fab fragment - light chain, ... (6 entities in total) |
| 機能のキーワード | anti-citrullinated protein antibody, collagen type ii, immune system |
| 由来する生物種 | Homo sapiens 詳細 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 48560.01 |
| 構造登録者 | |
| 主引用文献 | Kissel, T.,Ge, C.,Hafkenscheid, L.,Kwekkeboom, J.C.,Slot, L.M.,Cavallari, M.,He, Y.,van Schie, K.A.,Vergroesen, R.D.,Kampstra, A.S.B.,Reijm, S.,Stoeken-Rijsbergen, G.,Koeleman, C.,Voortman, L.M.,Heitman, L.H.,Xu, B.,Pruijn, G.J.M.,Wuhrer, M.,Rispens, T.,Huizinga, T.W.J.,Scherer, H.U.,Reth, M.,Holmdahl, R.,Toes, R.E.M. Surface Ig variable domain glycosylation affects autoantigen binding and acts as threshold for human autoreactive B cell activation. Sci Adv, 8:eabm1759-eabm1759, 2022 Cited by PubMed Abstract: The hallmark autoantibodies in rheumatoid arthritis are characterized by variable domain glycans (VDGs). Their abundant occurrence results from the selective introduction of N-linked glycosylation sites during somatic hypermutation, and their presence is predictive for disease development. However, the functional consequences of VDGs on autoreactive B cells remain elusive. Combining crystallography, glycobiology, and functional B cell assays allowed us to dissect key characteristics of VDGs on human B cell biology. Crystal structures showed that VDGs are positioned in the vicinity of the antigen-binding pocket, and dynamic modeling combined with binding assays elucidated their impact on binding. We found that VDG-expressing B cell receptors stay longer on the B cell surface and that VDGs enhance B cell activation. These results provide a rationale on how the acquisition of VDGs might contribute to the breach of tolerance of autoreactive B cells in a major human autoimmune disease. PubMed: 35138894DOI: 10.1126/sciadv.abm1759 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.85 Å) |
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