1FN4

CRYSTAL STRUCTURE OF FAB198, AN EFFICIENT PROTECTOR OF ACETYLCHOLINE RECEPTOR AGAINST MYASTHENOGENIC ANTIBODIES

Summary for 1FN4

• Entry DOI: 10.2210/pdb1fn4/pdb
• Descriptor: MONOCLONAL ANTIBODY AGAINST ACETYLCHOLINE RECEPTOR (3 entities in total)
• Functional Keywords: fab198, immune system
• Biological source: Rattus norvegicus (Norway rat); More
• Total number of polymer chains: 4
• Total formula weight: 93662.75

Authors

Poulas, K.,Eliopoulos, E.,Vatzaki, E.,Navaza, J.,Kontou, M. (deposition date: 2000-08-21, release date: 2001-09-26, Last modification date: 2024-11-06)

Primary citation

Poulas, K.,Eliopoulos, E.,Vatzaki, E.,Navaza, J.,Kontou, M.,Oikonomakos, N.,Acharya, K.R.,Tzartos, S.J.
Crystal structure of Fab198, an efficient protector of the acetylcholine receptor against myasthenogenic antibodies.
Eur.J.Biochem., 268:3685-3693, 2001

PubMed Abstract: The crystal structure of the Fab fragment of the rat monoclonal antibody 198, with protective activity for the main immunogenic region of the human muscle acetylcholine receptor against the destructive action of myasthenic antibodies, has been determined and refined to 2.8 A resolution by X-ray crystallographic methods. The mouse anti-lysozyme Fab D1.3 was used as a search model in molecular replacement with the AMORE software. The complementarity determining regions (CDR)-L2, CDR-H1 and CDR-H2 belong to canonical groups. Loops CDR-L3, CDR-H2 and CDR-H3, which seem to make a major contribution to binding, were analyzed and residues of potential importance for antigen-binding are examined. The antigen-binding site was found to be a long crescent-shaped crevice. The structure should serve as a model in the rational design of very high affinity humanized mutants of Fab198, appropriate for therapeutic approaches in the model autoimmune disease myasthenia gravis.

PubMed: 11432734
DOI: 10.1046/j.1432-1327.2001.02274.x

Experimental method

X-RAY DIFFRACTION (2.8 Å)