1kem
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The x-ray crystal structures of the sulfide oxidase antibody 28B4 and of | + | The x-ray crystal structures of the sulfide oxidase antibody 28B4 and of antibody 28B4 complexed with hapten have been solved at 2.2-angstrom and 1.9-angstrom resolution, respectively. To our knowledge, these structures are the highest resolution catalytic antibody structures to date and provide insight into the molecular mechanism of this antibody-catalyzed monooxygenation reaction. Specifically, the data suggest that entropic restriction plays a fundamental role in catalysis through the precise alignment of the thioether substrate and oxidant. The antibody active site also stabilizes developing charge on both sulfur and periodate in the transition state via cation-pi and electrostatic interactions, respectively. In addition to demonstrating that the active site of antibody 28B4 does indeed reflect the mechanistic information programmed in the aminophosphonic acid hapten, these high-resolution structures provide a basis for enhancing turnover rates through mutagenesis and improved hapten design. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Hsieh-Wilson, L | + | [[Category: Hsieh-Wilson, L C.]] |
| - | [[Category: Schultz, P | + | [[Category: Schultz, P G.]] |
| - | [[Category: Stevens, R | + | [[Category: Stevens, R C.]] |
[[Category: catalytic antibody]] | [[Category: catalytic antibody]] | ||
[[Category: fab]] | [[Category: fab]] | ||
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[[Category: sulfide oxidation]] | [[Category: sulfide oxidation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:33:15 2008'' |
Revision as of 11:33, 21 February 2008
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CATALYTIC ANTIBODY 28B4 FAB FRAGMENT
Overview
The x-ray crystal structures of the sulfide oxidase antibody 28B4 and of antibody 28B4 complexed with hapten have been solved at 2.2-angstrom and 1.9-angstrom resolution, respectively. To our knowledge, these structures are the highest resolution catalytic antibody structures to date and provide insight into the molecular mechanism of this antibody-catalyzed monooxygenation reaction. Specifically, the data suggest that entropic restriction plays a fundamental role in catalysis through the precise alignment of the thioether substrate and oxidant. The antibody active site also stabilizes developing charge on both sulfur and periodate in the transition state via cation-pi and electrostatic interactions, respectively. In addition to demonstrating that the active site of antibody 28B4 does indeed reflect the mechanistic information programmed in the aminophosphonic acid hapten, these high-resolution structures provide a basis for enhancing turnover rates through mutagenesis and improved hapten design.
About this Structure
1KEM is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Insights into antibody catalysis: structure of an oxygenation catalyst at 1.9-angstrom resolution., Hsieh-Wilson LC, Schultz PG, Stevens RC, Proc Natl Acad Sci U S A. 1996 May 28;93(11):5363-7. PMID:8643580
Page seeded by OCA on Thu Feb 21 13:33:15 2008
