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An Unprecedented Catalytic Motif Revealed in the Model Structure of Amide Hydrolyzing Antibody 312d6
Author(s) -
Benedetti Fabio,
Berti Federico,
Brady Kevin,
Colombatti Alfonso,
Pauletto Alessandro,
Pucillo Carlo,
Thomas Neil R.
Publication year - 2004
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200300738
Subject(s) - hapten , catalysis , chemistry , antibody , computational biology , stereochemistry , amide , docking (animal) , homology modeling , structural motif , motif (music) , combinatorial chemistry , dyad , biochemistry , biology , enzyme , genetics , psychology , medicine , philosophy , aesthetics , social psychology , nursing
An arginine dyad: A homology model of catalytic antibody 312D6 sets the rationale for the antibod y 's amidase activity. Docking of a sulfonamide hapten to the model highlights the role of an arginine dyad in binding and catalysis. This catalytic motif is unprecedented in antibody catalysis.