1a0q
From Proteopedia
(New page: 200px<br /> <applet load="1a0q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a0q, resolution 2.3Å" /> '''29G11 COMPLEXED WITH...) |
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| - | [[Image:1a0q.gif|left|200px]]<br /> | + | [[Image:1a0q.gif|left|200px]]<br /><applet load="1a0q" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1a0q" size=" | + | |
caption="1a0q, resolution 2.3Å" /> | caption="1a0q, resolution 2.3Å" /> | ||
'''29G11 COMPLEXED WITH PHENYL [1-(1-N-SUCCINYLAMINO)PENTYL] PHOSPHONATE'''<br /> | '''29G11 COMPLEXED WITH PHENYL [1-(1-N-SUCCINYLAMINO)PENTYL] PHOSPHONATE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystallographic structure of the Fab fragment of the catalytic | + | The crystallographic structure of the Fab fragment of the catalytic antibody, 29G11, complexed with an (S)-norleucine phenyl phosphonate transition state analog was determined at 2.2 A resolution. The antibody catalyzes the hydrolysis of norleucine phenyl ester with (S)-enantioselectivity. The shape and charge complementarity of the binding pocket for the hapten account for the preferential binding of the (S)-enantiomer of the substrate. The structure is compared to that of the more catalytically efficient antibody, 17E8, induced by the same hapten transition state analog. 29G11 has different residues from 17E8 at eight positions in the heavy chain, including four substitutions in the hapten-binding pocket: A33V, S95G, S99R and Y100AN, and four substitutions at positions remote from the catalytic site, I28T, R40K, V65G and F91L. The two antibodies show large differences in the orientations of their variable and constant domains, reflected by a 32 degrees difference in their elbow angles. The VL and VH domains in the two antibodies differ by a rotation of 8.8 degrees. The hapten binds in similar orientations and locations in 29G11 and 17E8, which appear to have catalytic groups in common, though the changes in the association of the variable domains affect the precise positioning of residues in the hapten-binding pocket. |
==About this Structure== | ==About this Structure== | ||
| - | 1A0Q is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ZN and HEP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1A0Q is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=HEP:'>HEP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A0Q OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Buchbinder, J | + | [[Category: Buchbinder, J L.]] |
| - | [[Category: Fletterick, R | + | [[Category: Fletterick, R J.]] |
| - | [[Category: Scanlan, T | + | [[Category: Scanlan, T S.]] |
| - | [[Category: Stephenson, R | + | [[Category: Stephenson, R C.]] |
[[Category: HEP]] | [[Category: HEP]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: esterase]] | [[Category: esterase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:39:34 2008'' |
Revision as of 09:39, 21 February 2008
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29G11 COMPLEXED WITH PHENYL [1-(1-N-SUCCINYLAMINO)PENTYL] PHOSPHONATE
Overview
The crystallographic structure of the Fab fragment of the catalytic antibody, 29G11, complexed with an (S)-norleucine phenyl phosphonate transition state analog was determined at 2.2 A resolution. The antibody catalyzes the hydrolysis of norleucine phenyl ester with (S)-enantioselectivity. The shape and charge complementarity of the binding pocket for the hapten account for the preferential binding of the (S)-enantiomer of the substrate. The structure is compared to that of the more catalytically efficient antibody, 17E8, induced by the same hapten transition state analog. 29G11 has different residues from 17E8 at eight positions in the heavy chain, including four substitutions in the hapten-binding pocket: A33V, S95G, S99R and Y100AN, and four substitutions at positions remote from the catalytic site, I28T, R40K, V65G and F91L. The two antibodies show large differences in the orientations of their variable and constant domains, reflected by a 32 degrees difference in their elbow angles. The VL and VH domains in the two antibodies differ by a rotation of 8.8 degrees. The hapten binds in similar orientations and locations in 29G11 and 17E8, which appear to have catalytic groups in common, though the changes in the association of the variable domains affect the precise positioning of residues in the hapten-binding pocket.
About this Structure
1A0Q is a Protein complex structure of sequences from Mus musculus with and as ligands. Full crystallographic information is available from OCA.
Reference
A comparison of the crystallographic structures of two catalytic antibodies with esterase activity., Buchbinder JL, Stephenson RC, Scanlan TS, Fletterick RJ, J Mol Biol. 1998 Oct 9;282(5):1033-41. PMID:9753552
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