Crystallographic Structural Studies of a Human Fc-Fragment. I. An Electron-Density Map at 4 Å Resolution and a Partial Model
- 1 January 1976
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 357 (1) , 435-446
- https://doi.org/10.1515/bchm2.1976.357.1.435
Abstract
The crystal structure of a human Fc fragment was analyzed at 4 .ANG. resolution. A partial interpretation of the electron-density map in terms of domain structure was possible. The molecule has the shape of a mickey mouse. The spherical domain was interpreted visually and by domain Patterson function interpretation as the CH3 [H chain constant region 3] dimer. This dimer resembles closely the CH1-CL dimer found in Fab structures. The ellipsoidal ears of the molecule represent the CH2 domains. They are widely separated from each other, but closely connected to CH3. Their tertiary structure must be different from CH1, as Patterson domain interpretations were unsuccessful. A chain tracing in CH2 was not yet possible.This publication has 12 references indexed in Scilit:
- Structure of the human antibody molecule kol (immunoglobulin G1): An electron density map at 5 Å resolutionJournal of Molecular Biology, 1976
- Three-Dimensional Structure of ImmunoglobulinsAnnual Review of Biochemistry, 1975
- ComplementAnnual Review of Biochemistry, 1975
- Refinement of setting angles in screenless film methodsJournal of Applied Crystallography, 1975
- The Three-Dimensional Structure of a Phosphorylcholine-Binding Mouse Immunoglobulin Fab and the Nature of the Antigen Binding SiteProceedings of the National Academy of Sciences, 1974
- The Three Dimensional Structure of a Combining Region-Ligand Complex of Immunoglobulin NEW at 3.5-Å ResolutionProceedings of the National Academy of Sciences, 1974
- Crystal Structure of an Immunoglobulin Molecule by X-Ray Diffraction and Electron MicroscopyCold Spring Harbor Symposia on Quantitative Biology, 1972
- Kristallisation des mit Plasmin erhaltenen Fe-Fragments aus Human-IgG-GlobulinKlinische Wochenschrift, 1969
- Human Fc fragment: Crystallographic evidence for two equivalent subunitsJournal of Molecular Biology, 1968
- Crystallographic study of human myeloma Fc-fragmentJournal of Molecular Biology, 1967