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PDBsum entry 4w4o
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Immune system
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PDB id
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4w4o
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References listed in PDB file
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Key reference
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Title
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Structural basis for binding of human igg1 to its high-Affinity human receptor fcγri.
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Authors
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M.Kiyoshi,
J.M.Caaveiro,
T.Kawai,
S.Tashiro,
T.Ide,
Y.Asaoka,
K.Hatayama,
K.Tsumoto.
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Ref.
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Nat Commun, 2015,
6,
6866.
[DOI no: ]
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PubMed id
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Abstract
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Cell-surface Fcγ receptors mediate innate and adaptive immune responses. Human
Fcγ receptor I (hFcγRI) binds IgGs with high affinity and is the only Fcγ
receptor that can effectively capture monomeric IgGs. However, the molecular
basis of hFcγRI's interaction with Fc has not been determined, limiting our
understanding of this major immune receptor. Here we report the crystal
structure of a complex between hFcγRI and human Fc, at 1.80 Å resolution,
revealing an unique hydrophobic pocket at the surface of hFcγRI perfectly
suited for residue Leu235 of Fc, which explains the high affinity of this
complex. Structural, kinetic and thermodynamic data demonstrate that the binding
mechanism is governed by a combination of non-covalent interactions, bridging
water molecules and the dynamic features of Fc. In addition, the hinge region of
hFcγRI-bound Fc adopts a straight conformation, potentially orienting the Fab
moiety. These findings will stimulate the development of novel therapeutic
strategies involving hFcγRI.
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