1c5c
From Proteopedia
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| - | + | {{STRUCTURE_1c5c| PDB=1c5c | SCENE= }} | |
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'''DECARBOXYLASE CATALYTIC ANTIBODY 21D8-HAPTEN COMPLEX''' | '''DECARBOXYLASE CATALYTIC ANTIBODY 21D8-HAPTEN COMPLEX''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C5C OCA]. | |
==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/11183784 11183784] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11183784 11183784] | ||
| - | [[Category: Mus musculus + homo sapiens]] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Hotta, K.]] | [[Category: Hotta, K.]] | ||
[[Category: Wilson, I A.]] | [[Category: Wilson, I A.]] | ||
| - | [[Category: | + | [[Category: Catalytic antibody]] |
| - | [[Category: | + | [[Category: Chimeric fab]] |
| - | [[Category: | + | [[Category: Decarboxylase]] |
| - | [[Category: | + | [[Category: Hapten complex]] |
| - | [[Category: | + | [[Category: Immunoglobulin]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:20:48 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:20, 2 May 2008
DECARBOXYLASE CATALYTIC ANTIBODY 21D8-HAPTEN COMPLEX
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
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 Fri May 2 12:20:48 2008
