1c5b
From Proteopedia
(New page: 200px<br /> <applet load="1c5b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c5b, resolution 2.10Å" /> '''DECARBOXYLASE CATAL...) |
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| - | [[Image:1c5b.gif|left|200px]]<br /> | + | [[Image:1c5b.gif|left|200px]]<br /><applet load="1c5b" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1c5b" size=" | + | |
caption="1c5b, resolution 2.10Å" /> | caption="1c5b, resolution 2.10Å" /> | ||
'''DECARBOXYLASE CATALYTIC ANTIBODY 21D8 UNLIGANDED FORM'''<br /> | '''DECARBOXYLASE CATALYTIC ANTIBODY 21D8 UNLIGANDED FORM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Antibody 21D8 catalyzes the solvent-sensitive decarboxylation of | + | Antibody 21D8 catalyzes the solvent-sensitive decarboxylation of 3-carboxybenzisoxazoles. The crystal structure of chimeric Fab 21D8 with and without hapten at 1.61 A and 2.10 A, respectively, together with computational analysis, shows how a melange of polar and non-polar sites are exploited to achieve both substrate binding and acceleration of a reaction normally facilitated by purely aprotic dipolar media. The striking similarity of the decarboxylase and a series of unrelated esterase antibodies also highlights the chemical versatility of structurally conserved anion binding sites and the relatively subtle changes involved in fine-tuning the immunoglobulin pocket for recognition of different ligands and catalysis of different reactions. |
==About this Structure== | ==About this Structure== | ||
| - | 1C5B is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus_+_homo_sapiens Mus musculus + homo sapiens]. Full crystallographic information is available from [http:// | + | 1C5B is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus_+_homo_sapiens Mus musculus + homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C5B OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Hotta, K.]] | [[Category: Hotta, K.]] | ||
| - | [[Category: Wilson, I | + | [[Category: Wilson, I A.]] |
[[Category: catalytic antibody]] | [[Category: catalytic antibody]] | ||
[[Category: chimeric fab]] | [[Category: chimeric fab]] | ||
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[[Category: unliganded]] | [[Category: unliganded]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:02:31 2008'' |
Revision as of 10:02, 21 February 2008
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DECARBOXYLASE CATALYTIC ANTIBODY 21D8 UNLIGANDED FORM
Overview
Antibody 21D8 catalyzes the solvent-sensitive decarboxylation of 3-carboxybenzisoxazoles. The crystal structure of chimeric Fab 21D8 with and without hapten at 1.61 A and 2.10 A, respectively, together with computational analysis, shows how a melange of polar and non-polar sites are exploited to achieve both substrate binding and acceleration of a reaction normally facilitated by purely aprotic dipolar media. The striking similarity of the decarboxylase and a series of unrelated esterase antibodies also highlights the chemical versatility of structurally conserved anion binding sites and the relatively subtle changes involved in fine-tuning the immunoglobulin pocket for recognition of different ligands and catalysis of different reactions.
About this Structure
1C5B is a Protein complex structure of sequences from Mus musculus + homo sapiens. Full crystallographic information is available from OCA.
Reference
Catalysis of decarboxylation by a preorganized heterogeneous microenvironment: crystal structures of abzyme 21D8., Hotta K, Lange H, Tantillo DJ, Houk KN, Hilvert D, Wilson IA, J Mol Biol. 2000 Oct 6;302(5):1213-25. PMID:11183784
Page seeded by OCA on Thu Feb 21 12:02:31 2008
