Crystal structure of the human leukocyte Fc receptor, FcγRIIa

Fcγ receptors bind IgG to initiate cellular responses against pathogens and soluble antigens. We have determined the three–dimensional structure of the extracellular portion of human FcγRIIa to 2.0 Å resolution providing a structural basis for the unique functions of the leukocyte FcR family. The re...

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Veröffentlicht in:Nature Structural Biology 1999-05, Vol.6 (5), p.437-442
Hauptverfasser: Hogarth, P. Mark, Maxwell, Kelly F, Powell, Maree S, Hulett, Mark D, Barton, Peter A, McKenzie, Ian F. C, Garrett, Thomas P.J
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container_issue 5
container_start_page 437
container_title Nature Structural Biology
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creator Hogarth, P. Mark
Maxwell, Kelly F
Powell, Maree S
Hulett, Mark D
Barton, Peter A
McKenzie, Ian F. C
Garrett, Thomas P.J
description Fcγ receptors bind IgG to initiate cellular responses against pathogens and soluble antigens. We have determined the three–dimensional structure of the extracellular portion of human FcγRIIa to 2.0 Å resolution providing a structural basis for the unique functions of the leukocyte FcR family. The receptor is composed of two immunoglobulin domains and arranged to expose the ligand–binding site at one end of domain 2. Using alanine mutants we find that the binding sites for IgG1 and 2 are similar but the relative importance of specific regions on the receptor varies. In crystals, FcγRIIa molecules associate to resemble V L V H dimers, suggesting that two FcγRIIa molecules could cooperate to bind IgG in an asymmetric manner.
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subjects Biochemistry
Biological Microscopy
Biomedical and Life Sciences
letter
Life Sciences
Membrane Biology
Protein Structure
title Crystal structure of the human leukocyte Fc receptor, FcγRIIa
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