1FRT

CRYSTAL STRUCTURE OF THE COMPLEX OF RAT NEONATAL FC RECEPTOR WITH FC

Summary for 1FRT

• Entry DOI: 10.2210/pdb1frt/pdb
• Descriptor: NEONATAL FC RECEPTOR, BETA 2-MICROGLOBULIN, IGG FC, ... (6 entities in total)
• Functional Keywords: complex (receptor-immunoglobulin), complex (receptor-immunoglobulin) complex, complex (receptor/immunoglobulin)
• Biological source: Rattus norvegicus (Norway rat); More
• Total number of polymer chains: 3
• Total formula weight: 67611.76

Authors

Burmeister, W.P.,Bjorkman, P.J. (deposition date: 1994-11-11, release date: 1995-02-14, Last modification date: 2024-12-25)

Primary citation

Burmeister, W.P.,Huber, A.H.,Bjorkman, P.J.
Crystal structure of the complex of rat neonatal Fc receptor with Fc.
Nature, 372:379-383, 1994

PubMed Abstract: The neonatal Fc receptor (FcRn) transports maternal immunoglobulin G (IgG) to the bloodstream of the newborn. FcRn is structurally similar to class I major histocompatibility complex (MHC) molecules, despite differences in the ligands they bind (the Fc portion of IgG and antigenic peptides, respectively). A low-resolution crystal structure of the complex between FcRn and Fc localizes the binding site for Fc to the side of FcRn, distinct from the tops of the alpha 1 and alpha 2 domains which serve as the peptide and T-cell receptor binding sites in class I molecules. FcRn binds to Fc at the interface between the Fc CH2 and CH3 domains, which contains several histidine residues that could account for the sharply pH-dependent FcRn/IgG interaction. A dimer of FcRn heterodimers observed in the co-crystals and in the crystals of FcRn alone could be involved in binding Fc, correlating with the 2:1 binding stoichiometry between FcRn and IgG (ref. 4) and suggesting an unusual orientation of FcRn on the membrane.

PubMed: 7969498
DOI: 10.1038/372379a0

Experimental method

X-RAY DIFFRACTION (4.5 Å)