Crystal structure of the human leukocyte Fc receptor, Fc gammaRIIa
| Autor: | K F, Maxwell, M S, Powell, M D, Hulett, P A, Barton, I F, McKenzie, T P, Garrett, P M, Hogarth |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Models
Molecular Binding Sites Protein Conformation Molecular Sequence Data Receptors IgG Immunoglobulins Crystallography X-Ray Ligands Transfection Amino Acid Substitution Antigens CD Immunoglobulin G COS Cells Leukocytes Animals Humans Amino Acid Sequence Crystallization Dimerization Conserved Sequence Protein Binding |
| Zdroj: | Nature structural biology. 6(5) |
| ISSN: | 1072-8368 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink