1yeh
From Proteopedia
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'''STRUCTURE OF IGG2A FAB FRAGMENT''' | '''STRUCTURE OF IGG2A FAB FRAGMENT''' | ||
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[[Category: Gigant, B.]] | [[Category: Gigant, B.]] | ||
[[Category: Knossow, M.]] | [[Category: Knossow, M.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:13:22 2008'' | |
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Revision as of 13:13, 3 May 2008
STRUCTURE OF IGG2A FAB FRAGMENT
Overview
The x-ray structures of the unliganded esterase-like catalytic antibody D2.3 and its complexes with a substrate analogue and with one of the reaction products are analyzed. Together with the structure of the phosphonate transition state analogue hapten complex, these crystal structures provide a complete description of the reaction pathway. At alkaline pH, D2.3 acts by preferential stabilization of the negatively charged oxyanion intermediate of the reaction that results from hydroxide attack on the substrate. A tyrosine residue plays a crucial role in catalysis: it activates the ester substrate and, together with an asparagine, it stabilizes the oxyanion intermediate. A canal allows facile diffusion of water molecules to the reaction center that is deeply buried in the structure. Residues bordering this canal provide targets for mutagenesis to introduce a general base in the vicinity of the reaction center.
About this Structure
1YEH is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
X-ray structures of a hydrolytic antibody and of complexes elucidate catalytic pathway from substrate binding and transition state stabilization through water attack and product release., Gigant B, Charbonnier JB, Eshhar Z, Green BS, Knossow M, Proc Natl Acad Sci U S A. 1997 Jul 22;94(15):7857-61. PMID:9223277 Page seeded by OCA on Sat May 3 16:13:22 2008
