1i1a: Difference between revisions
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'''CRYSTAL STRUCTURE OF THE NEONATAL FC RECEPTOR COMPLEXED WITH A HETERODIMERIC FC''' | '''CRYSTAL STRUCTURE OF THE NEONATAL FC RECEPTOR COMPLEXED WITH A HETERODIMERIC FC''' | ||
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[[Category: Jr., A P.West.]] | [[Category: Jr., A P.West.]] | ||
[[Category: Martin, W L.]] | [[Category: Martin, W L.]] | ||
[[Category: | [[Category: Ig constant domain]] | ||
[[Category: | [[Category: Mhc class i fold]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:27:22 2008'' | |||
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Revision as of 19:27, 2 May 2008
CRYSTAL STRUCTURE OF THE NEONATAL FC RECEPTOR COMPLEXED WITH A HETERODIMERIC FC
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. 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 Page seeded by OCA on Fri May 2 19:27:22 2008