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Identification of specificity‐determining residues in antibodies
Author(s) -
Padlan Eduardo A.,
Abergel Chantal,
Tipper Jennifer P.
Publication year - 1995
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.9.1.7821752
Subject(s) - antibody , complementarity (molecular biology) , computational biology , amino acid residue , peptide sequence , antigen , identification (biology) , chemistry , sequence (biology) , ligand (biochemistry) , complementarity determining region , biology , biochemistry , genetics , monoclonal antibody , receptor , botany , gene
The successful identification of the residues that contact ligand has important implications, especially in view of the increasing use of antibodies in various medical and industrial applications. Analysis of the crystallographically derived, three‐dimensional structures of five antibody‐antigen complexes and of the available amino acid sequence data on antibody variable regions reveals that the residues that contact antigen are in the main also the most variable. It is proposed that a good first guess of the identity of the specificity‐determining residues can be made from an examination of the variability values at sequence positions. New boundaries for the complementarity‐determining regions are proposed.—Padlan, E. A., Abergel, C., Tipper, J. P. Identification of specificity‐determining residues in antibodies. FASEB J. 9, 133‐139 (1995)