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TitleStructural differences between glycosylated, disulfide-linked heterodimeric Knob-into-Hole Fc fragment and its homodimeric Knob-Knob and Hole-Hole side products.
Journal, issue, pagesProtein Eng. Des. Sel., Vol. 30, Page 649-656, Year 2017
Publish dateFeb 1, 2016 (structure data deposition date)
AuthorsKuglstatter, A. / Stihle, M. / Neumann, C. / Muller, C. / Schaefer, W. / Klein, C. / Benz, J.
External linksProtein Eng. Des. Sel. / PubMed:28985438
MethodsX-ray diffraction
Resolution1.8 - 2.9 Å
Structure data

PDB-5hy9:
Glycosylated, disulfide-linked Knob-into-Hole Fc fragment
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-5hye:
Glycosylated Knob-Knob Fc fragment (P212121)
Method: X-RAY DIFFRACTION / Resolution: 1.89 Å

PDB-5hyf:
Glycosylated Knob-Knob Fc fragment (P6122)
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-5hyi:
Glycosylated, disulfide-linked Hole-Hole Fc fragment
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / Bispecific antibody Fc engineering Knob-into-Hole

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