1FCG
ECTODOMAIN OF HUMAN FC GAMMA RECEPTOR, FCGRIIA
Summary for 1FCG
| Entry DOI | 10.2210/pdb1fcg/pdb |
| Descriptor | PROTEIN (FC RECEPTOR FC(GAMMA)RIIA) (2 entities in total) |
| Functional Keywords | fc receptor, immunogloulin, leukocyte, cd32, immune system, membrane protein |
| 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 | 19556.86 |
| Authors | Maxwell, K.F.,Powell, M.S.,Garrett, T.P.,Hogarth, P.M. (deposition date: 1999-04-07, release date: 2000-04-12, Last modification date: 2024-10-16) |
| Primary citation | Maxwell, K.F.,Powell, M.S.,Hulett, M.D.,Barton, P.A.,McKenzie, I.F.,Garrett, T.P.,Hogarth, P.M. Crystal structure of the human leukocyte Fc receptor, Fc gammaRIIa. Nat.Struct.Biol., 6:437-442, 1999 Cited by PubMed Abstract: Fc gamma 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 Fc gammaRIIa to 2.0 A 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, Fc gammaRIIa molecules associate to resemble V(L)V(H) dimers, suggesting that two Fc gammaRIIa molecules could cooperate to bind IgG in an asymmetric manner. PubMed: 10331870DOI: 10.1038/8241 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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