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J. Biol. Chem., Vol. 276, Issue 19, 16469-16477, May 11, 2001
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From the Fc
The Structure of a Human Type III Fc
Receptor
in Complex with Fc*
,
Structural Biology Section, Laboratory of
Immunogenetics, NIAID, National Institutes of Health, Rockville,
Maryland 20852, the § Biochemistry, Cellular, and Molecular
Biology Program, Johns Hopkins University, School of Medicine,
Baltimore, Maryland 21205, and the ¶ Laboratory of Cellular and
Clinical Immunology, INSERM Unit 255, Curie Institute, 75005 Paris,
France
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 (FcRIIIB) in complex with an Fc
fragment of human IgG1 determined from orthorhombic and hexagonal
crystal forms at 3.0- and 3.5-Å 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 FcRIII, including the BC, C'E, FG loops,
and the C' 
-strand, bind asymmetrically to the lower hinge region,
residues Leu234-Pro238, 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 FcRIII·Fc and
Fc
RI·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 Asn297 on Fc may stabilize
the conformation of the receptor-binding epitope on Fc. An
antibody-FcRIII model suggests two possible ligand-induced receptor aggregations.
*
This work was supported by the intramural research funding
of NIAID, National Institutes of Health and by INSERM, Institut Curie,
France.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Structural Biology
Section, Laboratory of Immunogenetics, NIAID, National Institutes of
Health, 12441 Parklawn Dr., Rockville, MD 20852. Tel.: 301-496-3230; Fax: 301-402-0284; E-mail: psun@nih.gov.
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