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• W2013943906 abstract "The recognition of the Lex antigen by the anti-Lex monoclonal antibody (mAb) SH1 was studied by ELISA using a panel of 4″-modified Lex analogues. We confirmed that these analogues maintained the stacked conformation adopted by natural Lex antigen using 1D ROESY experiments and measuring intramolecular distances. Our binding studies show that the 4-OH″ of galactose behaves as an H-bond donor to an electronegative amino acid side chain in the SH1 binding site. While removal of this H-bond leads to reduced inhibition, disturbing the hydrophobic α face of the β-galactosyl residue leads to complete loss of binding to SH1. We compared our results to the crystal structure of the Fab fragment of anti-Lex mAb 291-2G3-A complexed with Lex (PDB entry 1UZ8). While no H-bond involving the 4-OH″ was described, hydrophobic interactions between a tryptophan residue and the β-galactoside α face are observed. We conclude that the hydrophobic α face that is uniquely displayed by β-galactosyl residues is essential to the recognition of the Lex antigen by anti-Lex antibodies." @default.
• W2013943906 created "2016-06-24" @default.
• W2013943906 creator A5067484626 @default.
• W2013943906 creator A5077890997 @default.
• W2013943906 date "2013-10-07" @default.
• W2013943906 modified "2023-10-18" @default.
• W2013943906 title "Understanding the Recognition of Lewis X by Anti-Le^x Monoclonal Antibodies" @default.
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• W2013943906 doi "https://doi.org/10.1021/jm401304h" @default.
• W2013943906 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24059473" @default.
• W2013943906 hasPublicationYear "2013" @default.
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