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. 1977 Nov;74(11):5140–5144. doi: 10.1073/pnas.74.11.5140

Three-dimensional structure of an intact human immunoglobulin.

E W Silverton, M A Navia, D R Davies
PMCID: PMC432116  PMID: 270751

Abstract

We have examined the low-resolution structure of a complete human IgG1 using known domain coordinates from crystallographic investigations of immunoglobulin fragment structures. Our results indicate that the Fc portion of this molecule has a structure similar to that of an isolated Fc fragment, with the carbohydrate moiety playing a central role as the principal contact between the CH2 domains. Carbohydrate also forms a large part of the interface between the Fc and Fab regions. The relative orientations of the variable and constant portions of the Fab regions are intermediate between those reported previously, emphasizing the flexibility of the switch region. These data do not support a two-state allosteric model such as has been proposed for antibody effector functions.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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