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Structure of a single-chain antibody variable domain (Fv) fragment complexed with a carbohydrate antigen at 1.7-Å resolution

From National Research Council Canada

Linkhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC44214/
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Affiliation
  1. National Research Council of Canada. NRC Biotechnology Research Institute
  2. National Research Council of Canada. NRC Institute for Biological Sciences
FormatText, Article
Subjectpharmaceutical
Abstract
We describe here the 1.7-Å resolution structure of a single-chain antibody variable domain (scFv) molecule, based on the carbohydrate-binding antibody Se155-4, complexed with the trisaccharide ligand α-D-Gal(1→2)[α-D-Abe(1→3)]α-D-Manp1→OMe, where Abe is abequose. The scFv expressed in Escherichia coli has the variable region light chain to heavy chain polarity with the domains connected by a 19-residue linker. Although the linker is partially disordered in the crystal, the packing of the molecules suggests a monomeric state of the scFv. The carbohydrate adopts a different conformation about the Man-Gal linkage than was observed previously in the Fab-trisaccharide complex. Instead of a direct hydrogen bond between O2Abe and O2Gal, these two atoms are bridged by a water molecule in the present complex.
Publication date
In
  • Proceedings of the National Academy of Sciences of the United States of America 91, no. 14 (5 July 1994): 6423–6427.
LanguageEnglish
NRC number36830
ZDANOV1994
NPARC number3538953
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Record identifier067b58d0-dc1d-4065-a74b-70800e2a1ef5
Record created2009-03-01
Record modified2020-04-27
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