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1jgv
From Proteopedia
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'''STRUCTURAL BASIS FOR DISFAVORED ELIMINATION REACTION IN CATALYTIC ANTIBODY 1D4''' | '''STRUCTURAL BASIS FOR DISFAVORED ELIMINATION REACTION IN CATALYTIC ANTIBODY 1D4''' | ||
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[[Category: Lerner, R A.]] | [[Category: Lerner, R A.]] | ||
[[Category: Wilson, I A.]] | [[Category: Wilson, I A.]] | ||
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Revision as of 18:12, 2 May 2008
STRUCTURAL BASIS FOR DISFAVORED ELIMINATION REACTION IN CATALYTIC ANTIBODY 1D4
Overview
Murine antibody 1D4 selectively catalyzes a highly disfavored beta-elimination reaction. Crystal structures of unliganded 1D4 and 1D4 in complex with a transition-state analog (TSA) have elucidated a possible general base mode of catalysis. The structures of the unliganded and liganded Fabs were determined to 1.80 and 1.85 A resolution, respectively. The structure of the complex reveals a binding pocket with high shape complementarity to the TSA, which is recruited to coerce the substrate into the sterically demanding, eclipsed conformation that is required for catalysis. A histidine residue and two water molecules are likely involved in the catalysis. The structure supports either a concerted E2 or stepwise E1cB-like mechanism for elimination. Finally, the liganded 1D4 structure shows minor conformational rearrangements in CDR H2, indicative of induced-fit binding of the hapten. 1D4 has pushed the boundaries of antibody-mediated catalysis into the realm of disfavored reactions and, hence, represents an important milestone in the development of this technology.
About this Structure
1JGV is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural basis for a disfavored elimination reaction in catalytic antibody 1D4., Larsen NA, Heine A, Crane L, Cravatt BF, Lerner RA, Wilson IA, J Mol Biol. 2001 Nov 16;314(1):93-102. PMID:11724535 Page seeded by OCA on Fri May 2 21:12:22 2008
