1CLY

IGG FAB (HUMAN IGG1, KAPPA) CHIMERIC FRAGMENT (CBR96) COMPLEXED WITH LEWIS Y NONOATE METHYL ESTER

Summary for 1CLY

• Entry DOI: 10.2210/pdb1cly/pdb
• Related PRD ID: PRD_900054
• Descriptor: IGG FAB (HUMAN IGG1, KAPPA), alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose, METHYL NONANOATE (ESTER), ... (4 entities in total)
• Functional Keywords: immunoglobulin, immunoglobulin c region, glycoprotein, antib
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 48535.23

Authors

Sheriff, S.,Bajorath, J. (deposition date: 1995-03-15, release date: 1996-08-01, Last modification date: 2024-11-20)

Primary citation

Jeffrey, P.D.,Bajorath, J.,Chang, C.Y.,Yelton, D.,Hellstrom, I.,Hellstrom, K.E.,Sheriff, S.
The x-ray structure of an anti-tumour antibody in complex with antigen.
Nat.Struct.Biol., 2:466-471, 1995

PubMed Abstract: The crystal structures of the murine BR96 Fab and its human chimera have been determined in complex with the nonoate methyl ester derivative of Lewis Y (nLey) at 2.8 A and 2.5 A resolution, respectively. BR96 binds the carbohydrate in a large pocket which is formed by residues of all CDR loops except L2. The binding of the carbohydrate is mediated predominantly by aromatic residues in BR96. Analysis of the structure suggests that BR96 is capable of recognizing a structure larger than the Le(y) tetrasaccharide, providing a possible explanation for its high tumour selectivity. The structure provides a rationale for mutagenesis experiments that have resulted in BR96 CDR loop mutants with increased affinity for nLey and/or tumour cells.

PubMed: 7664109
DOI: 10.1038/nsb0695-466

Experimental method

X-RAY DIFFRACTION (2.5 Å)