Carbohydrate and domain architecture of an immature antibody glycoform exhibiting enhanced effector functions

Max Crispin, Thomas A Bowden, Charlotte H Coles, Karl Harlos, Alexandru R Aricescu, D J Harvey, David I Stuart, E. Yvonne Jones

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

Antibodies contain a conserved glycosylation site that has emerged as a target for the modulation of antibody effector functions. The crystal structure of a biosynthetic intermediate of human IgG1, bearing immature oligomannose-type glycans and reported to display increased antibody-dependent cellular cytotoxicity, demonstrates that glycan engineering can bias the Fc to an open conformation primed for receptor binding.
Original languageEnglish
Pages (from-to)1061-6
Number of pages6
JournalJournal of Molecular Biology
Volume387
Issue number5
DOIs
Publication statusPublished - 17 Apr 2009

Keywords / Materials (for Non-textual outputs)

  • Antibody-Dependent Cell Cytotoxicity
  • Carbohydrate Sequence
  • Crystallography, X-Ray
  • Glycosylation
  • Humans
  • Immunoglobulin Fc Fragments
  • Immunoglobulin G
  • Models, Molecular
  • Oligosaccharides
  • Protein Structure, Tertiary
  • Recombinant Proteins
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Static Electricity

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