Crystallographic structure studies of an IgG molecule and an Fc fragment

  title={Crystallographic structure studies of an IgG molecule and an Fc fragment},
  author={Robert Huber and Johann Deisenhofer and Peter M. Colman and Masaaki Matsushima and Walter Palm},
The crystal structures of a human IgG antibody molecule Kol and a human Fc fragment have been determined at 4-Å and 3.5-Å resolution respectively, by isomorphous replacement. The electron-density maps were interpreted in terms of immunoglobulin domains based on the Rei and McPC 603 models (Kol) and by model-building (Fc). The Fab parts of Kol have a different quaternary structure from that observed in isolated crystalline Fab fragments, there being no longitudinal V–C contact in Kol. The Fc… 

Refined structure of an intact IgG2a monoclonal antibody.

The detailed structure of the IgG presented here, and the distribution of effector binding sites, appears consistent with effector activation mechanisms involving translocation and/or aggregation of the Fc following antigen binding by the Fabs.

The 3.2-Å crystal structure of the human IgG1 Fc fragment–FcγRIII complex

The described structure of a soluble Fcγ receptor (sFcγRIII, CD16), an Fc fragment from human IgG1 (hFc1) and their complex is a model for immune complex recognition and helps to explain the vastly differing affinities of other F cγR–IgG complexes and the FcεRIα-IgE complex.

Three-dimensional structure of an antigen-antibody complex at 2.8 A resolution

The 2.8 A resolution three-dimensional structure of a complex between an antigen (lysozyme) and the Fab fragment from a monoclonal antibody against lysozyme has been determined and refined by x-ray

Three-dimensional structure of an antibody-antigen complex.

The backbone structure of the antigen, lysozyme, is mostly unperturbed, although there are some changes in the epitope region, most notably Pro-70, and the Fab elbow bends in the two crystal forms differ by 7 degrees.



Crystallographic structural studies of a human Fc fragment. II. A complete model based on a Fourier map at 3.5 A resolution.

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, showing the immunoglobulin fold and the characteristic distribution of contact residues.

Crystallographic structural studies of a human Fc-fragment. I. An electron-density map at 4 A resolution and a partial model.

The crystal structure of a human Fc fragment was analysed at 4 A resolution. A partial interpretation of the electron-density map in terms of domain structure was possible. The molecule has the shape

Crystal and molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI.

The structure of the variable part of a χ-type Bence-Jones protein RE1 has been determined and the arrangement of the hypervariable segments especially in comparison with the Fab structure suggests that the V dimers form a primitive antibody.

The three-dimensional structure of a phosphorylcholine-binding mouse immunoglobulin Fab and the nature of the antigen binding site.

The structure of the Fab of McPC 603, a mouse myeloma protein with phosphorylcholine binding activity, has been determined to 3.1-A resoltuion. The four domains are found to be structurally similar

The three dimensional structure of a combining region-ligand complex of immunoglobulin NEW at 3.5-A resolution.

Binding studies indicate that both the 2-methylnaphthoquinone rings and the phytyl tail of the vitamin K(1) hapten contribute to the total binding energy.

The molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI refined at 2.0-A resolution.

The effects of hapten binding on the molecular structure can be analyzed by the difference Fourier technique with more reliability and the calculated phases based on the refined structure are much improved compared to isomorphous phases.

The three-dimensional structure at 6 A resolution of a human gamma Gl immunoglobulin molecule.

The electron density map has been calculated at 6 A resolution for a human γG1 immunoglobulin molecule and is interpreted in terms of four possible models, of which a T-shaped model is favored.

Conformational changes induced in a homogeneous anti-type III pneumococcal antibody by oligosaccharides of increasing size.

A multivalent ligand containing about 16 sugar residues appears to be the minimal antigenic size required for triggering conformational changes attributed to the Fc part, similar to those seen in the interaction with the whole polysaccharide antigen.