1fn4
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CRYSTAL STRUCTURE OF FAB198, AN EFFICIENT PROTECTOR OF ACETYLCHOLINE RECEPTOR AGAINST MYASTHENOGENIC ANTIBODIES
OverviewOverview
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.
About this StructureAbout this Structure
1FN4 is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of Fab198, an efficient protector of the acetylcholine receptor against myasthenogenic antibodies., Poulas K, Eliopoulos E, Vatzaki E, Navaza J, Kontou M, Oikonomakos N, Acharya KR, Tzartos SJ, Eur J Biochem. 2001 Jul;268(13):3685-93. PMID:11432734
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