1mfa

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spinqualitylabelsall models 1mfa, resolution 1.7Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURE OF A SINGLE-CHAIN FV FRAGMENT COMPLEXED WITH A CARBOHYDRATE ANTIGEN AT 1.7 ANGSTROMS RESOLUTION

Overview

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.

About this Structure

1MFA is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structure of a single-chain antibody variable domain (Fv) fragment complexed with a carbohydrate antigen at 1.7-A resolution., Zdanov A, Li Y, Bundle DR, Deng SJ, MacKenzie CR, Narang SA, Young NM, Cygler M, Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6423-7. PMID:7517550

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