Download MendeleyStructure of a single-chain antibody variable domain (Fv) fragment complexed with a carbohydrate antigen at 1.7-A resolution.
Zdanov, A., Li, Y., Bundle, D.R., Deng, S.J., MacKenzie, C.R., Narang, S.A., Young, N.M., Cygler, M.(1994) Proc Natl Acad Sci U S A 91: 6423-6427
- PubMed: 7517550
- DOI: https://doi.org/10.1073/pnas.91.14.6423
- Primary Citation of Related Structures:
1MFA - PubMed Abstract:
We describe here the 1.7-A resolution structure of a single-chain antibody variable domain (scFv) molecule, based on the carbohydrate-binding antibody Se155-4, complexed with the trisaccharide ligand alpha-D-Gal(1-->2)[alpha-D-Abe(1-->3)]alpha-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.
Organizational Affiliation:
Biotechnology Research Institute, National Research Council of Canada, Montreal, PQ.
