Summary for 3FRU
| Entry DOI | 10.2210/pdb3fru/pdb |
| Descriptor | NEONATAL FC RECEPTOR, BETA-2-MICROGLOBULIN, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total) |
| Functional Keywords | complex (immunoglobulin-binding protein), complex (immunoglobulin-binding protein) complex, complex (immunoglobulin/binding protein) |
| Biological source | Rattus norvegicus (Norway rat) More |
| Total number of polymer chains | 6 |
| Total formula weight | 129314.76 |
| Authors | Vaughn, D.E.,Burmeister, W.P.,Bjorkman, P.J. (deposition date: 1997-12-22, release date: 1998-06-10, Last modification date: 2025-03-26) |
| Primary citation | Vaughn, D.E.,Bjorkman, P.J. Structural basis of pH-dependent antibody binding by the neonatal Fc receptor. Structure, 6:63-73, 1998 Cited by PubMed Abstract: The neonatal Fc receptor (FcRn) mediates the transcytosis of maternal immunoglobulin G (IgG) across fetal and/or neonatal tissues for the acquisition of passive immunity. In adults, FcRn is involved in the maintenance of high serum IgG levels. Both processes are mediated by pH-dependent IgG binding to FcRn-FcRn binds to IgG with nanomolar affinity at pH 6, but shows no detectable binding at pH 7.5. At pH 6, FcRn is more thermally stable and the dissociation rate of its light chain is an order of magnitude slower than at pH 8.0. Comparison of the structures of FcRn at pH 6.5 and pH 8 allows an analysis of the structural basis for the receptor's pH-dependent ligand binding and stability. PubMed: 9493268DOI: 10.1016/S0969-2126(98)00008-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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