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Journal articles
Structure of a human IgA1 Fab fragment at 1.55 Å resolution: potential effect of the constant domains on antigen-affinity modulation.
Abstract : Despite being the most abundant class of immunoglobulins in humans and playing central roles in the adaptive immune response, high-resolution structural data are still lacking for the antigen-binding region of human isotype A antibodies (IgAs). The crystal structures of a human Fab fragment of IgA1 in three different crystal forms are now reported. The three-dimensional organization is similar to those of other Fab classes, but FabA1 seems to be more rigid, being constrained by a hydrophobic core in the interface between the variable and constant domains of the heavy chain (VH-CH1) as well as by a disulfide bridge that connects the light and heavy chains, influencing the relative heavy/light-chain orientation. The crystal structure of the same antibody but with a G-isotype CH1 which is reported to display different antigen affinity has also been solved. The differential structural features reveal plausible mechanisms for constant/variable-domain long-distance effects whereby antibody class switching could alter antigen affinity.
Cited literature [42 references]
https://hal-riip.archives-ouvertes.fr/pasteur-00847149
Contributor : Mariella Botta <>
Submitted on : Monday, July 22, 2013 - 5:09:20 PM
Last modification on : Friday, October 16, 2020 - 11:58:02 AM
Long-term archiving on: : Wednesday, April 5, 2017 - 4:36:11 PM
Contributor : Mariella Botta <>
Submitted on : Monday, July 22, 2013 - 5:09:20 PM
Last modification on : Friday, October 16, 2020 - 11:58:02 AM
Long-term archiving on: : Wednesday, April 5, 2017 - 4:36:11 PM
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