1h9v | pdb_00001h9v
HUMAN FC-GAMMA-RECEPTOR IIA (FCGRIIA), MONOCLINIC
| |||||||||||||
| 1h9v, resolution 3.0Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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.
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
Page seeded by OCA on Sun Mar 30 21:00:45 2008
