Contrasting IgG structures reveal extreme asymmetry and flexibility
Contrasting IgG structures reveal extreme asymmetry and flexibility
The crystal structure of IgG1 b12 represents the first visualization of an intact human IgG with a full-length hinge that has all domains ordered and visible. In comparison to intact murine antibodies and hinge-deletant human antibodies, b12 reveals extreme asymmetry, indicative of the extraordinary interdomain flexibility within an antibody. In addition, the structure provides an illustration of the human IgG1 hinge in its entirety and of asymmetry in the composition of the carbohydrate attached to each C(H)2 domain of the Fc. The two separate hinges assume different conformations in order to accommodate the vastly different placements of the two Fab domains relative to the Fc domain. Interestingly, only one of two possible intra-hinge disulfides is formed.
9-18
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
24 May 2002
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Crispin, Max
(2002)
Contrasting IgG structures reveal extreme asymmetry and flexibility.
Journal of Molecular Biology, 319 (1), .
(doi:10.1016/S0022-2836(02)00244-9).
Abstract
The crystal structure of IgG1 b12 represents the first visualization of an intact human IgG with a full-length hinge that has all domains ordered and visible. In comparison to intact murine antibodies and hinge-deletant human antibodies, b12 reveals extreme asymmetry, indicative of the extraordinary interdomain flexibility within an antibody. In addition, the structure provides an illustration of the human IgG1 hinge in its entirety and of asymmetry in the composition of the carbohydrate attached to each C(H)2 domain of the Fc. The two separate hinges assume different conformations in order to accommodate the vastly different placements of the two Fab domains relative to the Fc domain. Interestingly, only one of two possible intra-hinge disulfides is formed.
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Published date: 24 May 2002
Identifiers
Local EPrints ID: 450245
URI: http://eprints.soton.ac.uk/id/eprint/450245
ISSN: 0022-2836
PURE UUID: eed9104e-ce5b-4737-9235-5208dfb7a6f8
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Date deposited: 16 Jul 2021 16:37
Last modified: 17 Mar 2024 03:47
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