1frt
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(New page: 200px<br /><applet load="1frt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1frt, resolution 4.5Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 13:05, 20 November 2007
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CRYSTAL STRUCTURE OF THE COMPLEX OF RAT NEONATAL FC RECEPTOR WITH FC
Overview
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.
About this Structure
1FRT is a Protein complex structure of sequences from Rattus norvegicus with NAG as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the complex of rat neonatal Fc receptor with Fc., Burmeister WP, Huber AH, Bjorkman PJ, Nature. 1994 Nov 24;372(6504):379-83. PMID:7969498
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