1kel: Difference between revisions

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==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.

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==

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[[Category: Mus musculus]]

[[Category: Protein complex]]

[[Category: Hsieh-Wilson, L.C.]]

[[Category: Hsieh-Wilson, L C.]]

[[Category: Schultz, P.G.]]

[[Category: Schultz, P G.]]

[[Category: Stevens, R.C.]]

[[Category: Stevens, R C.]]

[[Category: AAH]]

[[Category: catalytic antibody]]

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[[Category: sulfide oxidation]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 13: / Line 13: @@
 [[Category: Mus musculus]]
 [[Category: Protein complex]]
-[[Category: Hsieh-Wilson, L.C.]]
+[[Category: Hsieh-Wilson, L C.]]
-[[Category: Schultz, P.G.]]
+[[Category: Schultz, P G.]]
-[[Category: Stevens, R.C.]]
+[[Category: Stevens, R C.]]
 [[Category: AAH]]
 [[Category: catalytic antibody]]
@@ Line 24: / Line 24: @@
 [[Category: sulfide oxidation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:13:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:33:13 2008''