Crystallographic Structural Studies of a Human Fc Fragment. II. A Complete Model Based on a Fourier Map at 3.5 Å Resolution

Abstract

The crystal structure analysis of a human Fc fragment was pursued to 3.5 A resolution and a complete model was built and refined into the isomorphous Fourier map. The CH2 and CH3 domains show the immunoglobulin fold, with CH3 being closely similar to CH1, but CH2 intermediate in structure between V and CH3. The carbohydrate is rigidly attached to CH2, covering the C face. CH3 dimerizes as CH1-CL, but CH2 has no contact to the second chain. Residues involved in the lateral CH3-CH3 and the longitudinal CH3-CH2 contact are conserved in Ig classes and sub-classes. In IgM and IgE the two C-terminal domains also show this characteristic distribution of contact residues.