1MFA

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

Summary for 1MFA

• Entry DOI: 10.2210/pdb1mfa/pdb
• Descriptor: IGG1-LAMBDA SE155-4 FAB (LIGHT CHAIN), IGG1-LAMBDA SE155-4 FAB (HEAVY CHAIN), alpha-D-galactopyranose-(1-2)-[alpha-D-Abequopyranose-(1-3)]methyl alpha-D-mannopyranoside, ... (4 entities in total)
• Functional Keywords: immunoglobulin
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 2
• Total formula weight: 26997.89

Authors

Zdanov, A.,Cygler, M. (deposition date: 1993-10-25, release date: 1994-01-31, Last modification date: 2024-11-06)

Primary citation

Zdanov, A.,Li, Y.,Bundle, D.R.,Deng, S.J.,MacKenzie, C.R.,Narang, S.A.,Young, N.M.,Cygler, M.
Structure of a single-chain antibody variable domain (Fv) fragment complexed with a carbohydrate antigen at 1.7-A resolution.
Proc.Natl.Acad.Sci.USA, 91:6423-6427, 1994

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.

PubMed: 7517550
DOI: 10.1073/pnas.91.14.6423

Experimental method

X-RAY DIFFRACTION (1.7 Å)