1H9V
Human Fc-gamma-Receptor IIa (FcgRIIa), monoclinic
Summary for 1H9V
| Entry DOI | 10.2210/pdb1h9v/pdb |
| Related | 1FCG |
| Descriptor | LOW AFFINITY IMMUNOGLOBULIN GAMMA FC RECEPTOR II-A (1 entity in total) |
| Functional Keywords | immune system, membrane protein, fcr, fc-receptor, immunoglobulin, fcgr, fc-gamma-r |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Cell membrane; Single-pass type I membrane protein: P12318 |
| Total number of polymer chains | 1 |
| Total formula weight | 19342.65 |
| Authors | Sondermann, P.,Kaiser, J.,Jacob, U. (deposition date: 2001-03-21, release date: 2001-06-21, Last modification date: 2024-11-20) |
| Primary citation | Sondermann, P.,Kaiser, J.,Jacob, U. Molecular Basis for Immune Complex Recognition: A Comparison of Fc-Receptor Structures J.Mol.Biol., 309:737-, 2001 Cited by PubMed Abstract: 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. PubMed: 11397093DOI: 10.1006/JMBI.2001.4670 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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