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Contrasting IgG structures reveal extreme asymmetry and flexibility

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.
0022-2836
9-18
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9
Crispin, Max
cd980957-0943-4b89-b2b2-710f01f33bc9

Crispin, Max (2002) Contrasting IgG structures reveal extreme asymmetry and flexibility. Journal of Molecular Biology, 319 (1), 9-18. (doi:10.1016/S0022-2836(02)00244-9).

Record type: Article

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
ORCID for Max Crispin: ORCID iD orcid.org/0000-0002-1072-2694

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Date deposited: 16 Jul 2021 16:37
Last modified: 17 Jul 2021 01:57

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