| Literature DB >> 7969491 |
W P Burmeister1, L N Gastinel, N E Simister, M L Blum, P J Bjorkman.
Abstract
The three-dimensional structure of the rat neonatal Fc receptor (FcRn) is similar to the structure of molecules of the major histocompatibility complex (MHC). The counterpart of the MHC peptide-binding site is closed in FcRn, making the FcRn groove incapable of binding peptides. A dimer of FcRn heterodimers seen in the crystals may represent a receptor dimer that forms when the Fc portion of a single immunoglobulin binds. An alternative use of the MHC fold for immune recognition is indicated by the FcRn and FcRn/Fc co-crystal structures.Entities:
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Year: 1994 PMID: 7969491 DOI: 10.1038/372336a0
Source DB: PubMed Journal: Nature ISSN: 0028-0836 Impact factor: 49.962