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

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TypeArticle
Journal titleProceedings of the National Academy of Sciences of the United States of America
Volume91
Issue14
Pages64236427; # of pages: 5
Subjectpha
AbstractWe 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
Linkhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC44214/
LanguageEnglish
AffiliationNRC Biotechnology Research Institute; National Research Council Canada; NRC Institute for Biological Sciences
Peer reviewedNo
NRC number36830
ZDANOV1994
NPARC number3538953
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Record identifier067b58d0-dc1d-4065-a74b-70800e2a1ef5
Record created2009-03-01
Record modified2016-05-09
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