| Structural highlights
Publication Abstract from PubMed
The molecular basis of antibody 5E5, which recognizes the entire GalNAc unit as a primary epitope is disclosed. The antibody's contacts with the peptide are mostly limited to two residues, allowing it to show some degree of promiscuity. These findings open the door to the chemical design of peptide-mimetics for developing efficient anti-cancer vaccines and diagnostic tools.
Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody.,Macias-Leon J, Bermejo IA, Asin A, Garcia-Garcia A, Companon I, Jimenez-Moreno E, Coelho H, Mangini V, Albuquerque IS, Marcelo F, Asensio JL, Bernardes GJL, Joshi HJ, Fiammengo R, Blixt O, Hurtado-Guerrero R, Corzana F Chem Commun (Camb). 2020 Dec 8;56(96):15137-15140. doi: 10.1039/d0cc06349e. PMID:33211039[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Macías-León J, Bermejo IA, Asín A, García-García A, Compañón I, Jiménez-Moreno E, Coelho H, Mangini V, Albuquerque IS, Marcelo F, Asensio JL, Bernardes GJL, Joshi HJ, Fiammengo R, Blixt O, Hurtado-Guerrero R, Corzana F. Structural characterization of an unprecedented lectin-like antitumoral anti-MUC1 antibody. Chem Commun (Camb). 2020 Dec 8;56(96):15137-15140. PMID:33211039 doi:10.1039/d0cc06349e
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