Abstract
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 part C terminal to the hinge is disordered in the Kol crystals. It is suggested that the Kol molecule is flexible in solution, whereas fragments are rigid. In the Fc fragment both CH3 and CH2 show the immunoglobulin fold. The C H3 dimer aggregates as CH1-CL while C H2 are widely separated from each other. The carbohydrate bound to Fc is in fixed position. From these structures a hypothetical liganded antibody molecule has been constructed, which is assumed to be rigid.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 415-420 |
| Number of pages | 6 |
| Journal | Nature |
| Volume | 264 |
| Issue number | 5585 |
| DOIs | |
| State | Published - 1976 |
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Crystallographic structure studies of an IgG molecule and an Fc fragment. / Huber, Robert; Deisenhofer, Johann; Colman, Peter M.; Matsushima, Masaaki; Palm, Walter.
In: Nature, Vol. 264, No. 5585, 1976, p. 415-420.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Crystallographic structure studies of an IgG molecule and an Fc fragment
AU - Huber, Robert
AU - Deisenhofer, Johann
AU - Colman, Peter M.
AU - Matsushima, Masaaki
AU - Palm, Walter
PY - 1976
Y1 - 1976
N2 - 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 part C terminal to the hinge is disordered in the Kol crystals. It is suggested that the Kol molecule is flexible in solution, whereas fragments are rigid. In the Fc fragment both CH3 and CH2 show the immunoglobulin fold. The C H3 dimer aggregates as CH1-CL while C H2 are widely separated from each other. The carbohydrate bound to Fc is in fixed position. From these structures a hypothetical liganded antibody molecule has been constructed, which is assumed to be rigid.
AB - 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 part C terminal to the hinge is disordered in the Kol crystals. It is suggested that the Kol molecule is flexible in solution, whereas fragments are rigid. In the Fc fragment both CH3 and CH2 show the immunoglobulin fold. The C H3 dimer aggregates as CH1-CL while C H2 are widely separated from each other. The carbohydrate bound to Fc is in fixed position. From these structures a hypothetical liganded antibody molecule has been constructed, which is assumed to be rigid.
UR - http://www.scopus.com/inward/record.url?scp=0017152608&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0017152608&partnerID=8YFLogxK
U2 - 10.1038/264415a0
DO - 10.1038/264415a0
M3 - Article
C2 - 1004567
AN - SCOPUS:0017152608
VL - 264
SP - 415
EP - 420
JO - Nature
JF - Nature
SN - 0028-0836
IS - 5585
ER -