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1h9v

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==Overview==
==Overview==
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Once antigen is opsonised by IgG it is removed from the circulation by, Fcgamma-receptor expressing cells. Fcgamma-receptors are type I, transmembrane molecules that carry extracellular parts consisting of two, or three immunoglobulin domains. Previously solved structures of, Fc-receptors reveal that the N-terminal two Ig-like domains are arranged, in a steep angle forming a heart-shaped structure. The crystal structure, of the FcgammaRIII/hIgG1-Fc-fragment demonstrated that the Fc-fragment is, recognised through loops of the C-terminal receptor domain of the, FcgammaRIII. As the overall structure of the FcRs and their Ig ligands are, very similar we modelled the Ig complexes with FcgammaRI, FcgammaRII and, FcepsilonRIalpha based on the FcgammaRIII/hIgG1-Fc-fragment structure. The, obtained models are consistent with the observed biochemical data and may, explain the observed specificity and affinities.
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Once antigen is opsonised by IgG it is removed from the circulation by Fcgamma-receptor expressing cells. Fcgamma-receptors are type I transmembrane molecules that carry extracellular parts consisting of two or three immunoglobulin domains. Previously solved structures of Fc-receptors reveal that the N-terminal two Ig-like domains are arranged in a steep angle forming a heart-shaped structure. The crystal structure of the FcgammaRIII/hIgG1-Fc-fragment demonstrated that the Fc-fragment is recognised through loops of the C-terminal receptor domain of the FcgammaRIII. As the overall structure of the FcRs and their Ig ligands are very similar we modelled the Ig complexes with FcgammaRI, FcgammaRII and FcepsilonRIalpha based on the FcgammaRIII/hIgG1-Fc-fragment structure. The obtained models are consistent with the observed biochemical data and may explain the observed specificity and affinities.
==Disease==
==Disease==
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Known diseases associated with this structure: Lupus nephritis, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=146790 146790]]
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Known diseases associated with this structure: Lupus nephritis, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=146790 146790]], Malaria, resistance to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604590 604590]], Systemic lupus erythematosus, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604590 604590]]
==About this Structure==
==About this Structure==
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[[Category: immunoglobulin]]
[[Category: immunoglobulin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:55:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:59:06 2008''

Revision as of 10:59, 21 February 2008


1h9v, resolution 3.0Å

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HUMAN FC-GAMMA-RECEPTOR IIA (FCGRIIA), MONOCLINIC

Contents

Overview

Once antigen is opsonised by IgG it is removed from the circulation by Fcgamma-receptor expressing cells. Fcgamma-receptors are type I transmembrane molecules that carry extracellular parts consisting of two or three immunoglobulin domains. Previously solved structures of Fc-receptors reveal that the N-terminal two Ig-like domains are arranged in a steep angle forming a heart-shaped structure. The crystal structure of the FcgammaRIII/hIgG1-Fc-fragment demonstrated that the Fc-fragment is recognised through loops of the C-terminal receptor domain of the FcgammaRIII. As the overall structure of the FcRs and their Ig ligands are very similar we modelled the Ig complexes with FcgammaRI, FcgammaRII and FcepsilonRIalpha based on the FcgammaRIII/hIgG1-Fc-fragment structure. The obtained models are consistent with the observed biochemical data and may explain the observed specificity and affinities.

Disease

Known diseases associated with this structure: Lupus nephritis, susceptibility to OMIM:[146790], Malaria, resistance to OMIM:[604590], Systemic lupus erythematosus, susceptibility to OMIM:[604590]

About this Structure

1H9V is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Molecular basis for immune complex recognition: a comparison of Fc-receptor structures., Sondermann P, Kaiser J, Jacob U, J Mol Biol. 2001 Jun 8;309(3):737-49. PMID:11397093

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