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* Residue conservation analysis
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PDB id:
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Immune system
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Title:
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Crystal structure of a human type iii fc gamma receptor in complex with an fc fragment of igg1 (orthorhombic)
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Structure:
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Igg1. Chain: a, b. Fragment: fc. Low affinity immunoglobulin gamma fc region receptor iii-b. Chain: c. Fragment: fc gamma receptor type iii. Synonym: igg fc receptor iii-1, fc-gamma riii-beta, fc-gamma riiib, fcriiib, fc-gamma riii, fcriii, cd16-b, fcr-10. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Biol. unit:
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Trimer (from
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Resolution:
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3.00Å
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R-factor:
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0.226
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R-free:
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0.282
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Authors:
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S.Radaev,S.Motyka,W.-H.Fridman,C.Sautes-Fridman,P.D.Sun
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Key ref:
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S.Radaev
et al.
(2001).
The structure of a human type III Fcgamma receptor in complex with Fc.
J Biol Chem,
276,
16469-16477.
PubMed id:
DOI:
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Date:
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11-May-04
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Release date:
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28-Sep-04
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Supersedes:
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PROCHECK
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Headers
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References
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DOI no:
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J Biol Chem
276:16469-16477
(2001)
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PubMed id:
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The structure of a human type III Fcgamma receptor in complex with Fc.
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S.Radaev,
S.Motyka,
W.H.Fridman,
C.Sautes-Fridman,
P.D.Sun.
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ABSTRACT
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Fcgamma receptors mediate antibody-dependent inflammatory responses and
cytotoxicity as well as certain autoimmune dysfunctions. Here we report the
crystal structure of a human Fc receptor (FcgammaRIIIB) in complex with an Fc
fragment of human IgG1 determined from orthorhombic and hexagonal crystal forms
at 3.0- and 3.5-A resolution, respectively. The refined structures from the two
crystal forms are nearly identical with no significant discrepancies between the
coordinates. Regions of the C-terminal domain of FcgammaRIII, including the BC,
C'E, FG loops, and the C' beta-strand, bind asymmetrically to the lower hinge
region, residues Leu(234)-Pro(238), of both Fc chains creating a 1:1
receptor-ligand stoichiometry. Minor conformational changes are observed in both
the receptor and Fc upon complex formation. Hydrophobic residues, hydrogen
bonds, and salt bridges are distributed throughout the receptor.Fc interface.
Sequence comparisons of the receptor-ligand interface residues suggest a
conserved binding mode common to all members of immunoglobulin-like Fc
receptors. Structural comparison between FcgammaRIII.Fc and FcepsilonRI.Fc
complexes highlights the differences in ligand recognition between the high and
low affinity receptors. Although not in direct contact with the receptor, the
carbohydrate attached to the conserved glycosylation residue Asn(297) on Fc may
stabilize the conformation of the receptor-binding epitope on Fc. An
antibody-FcgammaRIII model suggests two possible ligand-induced receptor
aggregations.
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Selected figure(s)
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Figure 6.
Fig. 6. Antibody-Fc  RIII
binding and ligand induced receptor aggregation model. A, an
intact antibody-Fc RIII
binding model. The structure of the antibody is shown in magenta
and that of Fc RIII is in
green. The position of the second possible orientation of Fc
RIII, which
is in direct steric conflict with the hinge region and Fab, is
indicated by a blue-shaded area. The arrow points to the
location of the lower hinge (L.H.). The Protein Data Bank entry
for the antibody coordinates is 1IGT. B, a simple avidity model
of antigen-antibody binding induced Fc RIII
aggregation. C, an ordered receptor aggregation model.
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Figure 7.
Fig. 7. Recognition of Fc by multiple ligands. Structural
comparison among the complexes of (A) Fc RIIIB-Fc;
(B) FcRn-Fc (PDB entry 1FRT); (C) rheumatoid factors RF-Fc (PDB
entry 1ADQ); and (D) bacterial protein A-Fc (PDB entry 1FC2).
Protein G binds similar to Fc as does protein A. Due to its
symmetric interaction with ligand, only one chain of Fc is shown
in the FcRn·Fc, RF·Fc and protein A·Fc
complexes. The corresponding Fc regions are colored in cyan and
shown in similar orientations. The ligands to Fc are colored in
green and the  [2]-microglobulin
of FcRn is shown in red. Only the variable domain of RF is
shown. The carbohydrates are shown in ball-and-stick models.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2001,
276,
16469-16477)
copyright 2001.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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P.M.Hogarth,
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NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic.
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PDB codes:
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PDB code:
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| |
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PDB code:
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| |
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| |
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| |
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P.M.Hogarth
(2002).
Fc receptors are major mediators of antibody based inflammation in autoimmunity.
|
| |
Curr Opin Immunol,
14,
798-802.
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S.Radaev,
B.Rostro,
A.G.Brooks,
M.Colonna,
and
P.D.Sun
(2001).
Conformational plasticity revealed by the cocrystal structure of NKG2D and its class I MHC-like ligand ULBP3.
|
| |
Immunity,
15,
1039-1049.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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