1i1a
CRYSTAL STRUCTURE OF THE NEONATAL FC RECEPTOR COMPLEXED WITH A HETERODIMERIC FC
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OverviewOverview
The neonatal Fc receptor (FcRn) transports immunoglobulin G (IgG) across, epithelia, binding IgG in acidic vesicles (pH < or = 6.5) and releasing, IgG in the blood at pH 7.4. Well-ordered FcRn/Fc crystals are prevented by, the formation of "oligomeric ribbons" of FcRn dimers bridged by Fc, homodimers, thus we crystallized a 1:1 complex between rat FcRn and a, heterodimeric Fc containing only one FcRn binding site. The 2.8 A complex, structure demonstrates that FcRn uses its alpha2 and beta2-microglobulin, domains and carbohydrate to interact with the Fc C(gamma)2-C(gamma)3, interface. The structure reveals conformational changes in Fc and three, titratable salt bridges that confer pH-dependent binding, and can be used, to guide rational design of therapeutic IgGs with longer serum half-lives.
About this StructureAbout this Structure
1I1A is a Protein complex structure of sequences from Rattus norvegicus with NDG, NAG and CYS as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure at 2.8 A of an FcRn/heterodimeric Fc complex: mechanism of pH-dependent binding., Martin WL, West AP Jr, Gan L, Bjorkman PJ, Mol Cell. 2001 Apr;7(4):867-77. PMID:11336709
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