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Thesis

Structural biology of IgG Fc glycoforms

Abstract:

The conserved N-linked glycosylation site on the Fc domain of IgG1 antibodies is essential for maintaining a functionally active conformation of the antibody. Different glycoforms of the Fc exhibit widely different effector functions. Similarly, therapeutic antibodies, with engineered glycosylation, exhibit altered binding to cellular Fc receptors (FcRs). Here, X-ray crystallographic structures were obtained for biosynthetic intermediate glycoforms of human IgG1 Fc bearing: unprocessed olig...

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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Research group:
Chris Scanlan
Oxford college:
Lincoln College
Role:
Author

Contributors

Division:
MSD
Department:
Biochemistry
Role:
Supervisor
Division:
MSD
Department:
Biochemistry
Role:
Supervisor
Publication date:
2012
Type of award:
DPhil
Level of award:
Doctoral
Awarding institution:
Oxford University, UK
Language:
English
Keywords:
Subjects:
UUID:
uuid:def683d3-aa06-41d9-9f28-29d21258bebe
Local pid:
ora:6307
Deposit date:
2012-06-21

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