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PDBsum entry 1frt
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Complex (receptor/immunoglobulin)
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PDB id
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1frt
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Contents |
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269 a.a.
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99 a.a.
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205 a.a.
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the complex of rat neonatal fc receptor with fc.
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Authors
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W.P.Burmeister,
A.H.Huber,
P.J.Bjorkman.
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Ref.
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Nature, 1994,
372,
379-383.
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PubMed id
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Abstract
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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.
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Secondary reference #1
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Title
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Crystal structure at 2.2 a resolution of the mhc-Related neonatal fc receptor.
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Authors
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W.P.Burmeister,
L.N.Gastinel,
N.E.Simister,
M.L.Blum,
P.J.Bjorkman.
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Ref.
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Nature, 1994,
372,
336-343.
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PubMed id
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Secondary reference #2
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Title
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Investigation of the interaction between the class i mhc-Related fc receptor and its immunoglobulin g ligand.
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Authors
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M.Raghavan,
M.Y.Chen,
L.N.Gastinel,
P.J.Bjorkman.
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Ref.
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Immunity, 1994,
1,
303-315.
[DOI no: ]
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PubMed id
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Figure 3.
igure 3. Comparisons of Binding Affinities of Wild-Type FcRn and
he FcRn Histidine and Loop Mutants for IgG
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Figure 7.
Figure 7. lAcore nalysis of he Inhibition of FcRn-IgG Interaction
by a Functional Analog of ragment of rotein A
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The above figures are
reproduced from the cited reference
with permission from Cell Press
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Secondary reference #3
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Title
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Crystallization and stoichiometry of binding of a complex between a rat intestinal fc receptor and fc.
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Authors
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A.H.Huber,
R.F.Kelley,
L.N.Gastinel,
P.J.Bjorkman.
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Ref.
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J Mol Biol, 1993,
230,
1077-1083.
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PubMed id
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Secondary reference #4
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Title
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Crystallographic refinement and atomic models of a human fc fragment and its complex with fragment b of protein a from staphylococcus aureus at 2.9- And 2.8-A resolution.
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Author
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J.Deisenhofer.
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Ref.
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Biochemistry, 1981,
20,
2361-2370.
[DOI no: ]
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PubMed id
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