1ngy

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|ACTIVITY=
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|GENE=
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|RELATEDENTRY=[[3fct|3FCT]], [[1n7m|1N7M]], [[1ngw|1NGW]], [[1ngx|1NGX]], [[1ngz|1NGZ]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ngy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ngy OCA], [http://www.ebi.ac.uk/pdbsum/1ngy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ngy RCSB]</span>
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[[Category: immunoglobulin]]
[[Category: immunoglobulin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:56:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:30:14 2008''

Revision as of 19:30, 30 March 2008


PDB ID 1ngy

Drag the structure with the mouse to rotate
, resolution 2.20Å
Related: 3FCT, 1N7M, 1NGW, 1NGX, 1NGZ


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Chimeric Mature Fab 7g12-Apo


Overview

The crystal structure of the Michaelis complex between the Fab fragment of ferrochelatase antibody 7G12 and its substrate mesoporphyrin has been solved to 2.6-A resolution. The antibody-bound mesoporphyrin clearly adopts a nonplanar conformation and reveals that the antibody catalyzes the porphyrin metallation reaction by straining/distorting the bound substrate toward the transition-state configuration. The crystal structures of the Fab fragment of the germ-line precursor antibody to 7G12 and its complex with the hapten N-methylmesoporphyrin have also been solved. A comparison of these structures with the corresponding structures of the affinity-matured antibody 7G12 reveals the molecular mechanism by which the immune system evolves binding energy to catalyze this reaction.

About this Structure

1NGY is a Protein complex structure of sequences from Mus musculus, homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural evidence for substrate strain in antibody catalysis., Yin J, Andryski SE, Beuscher AE 4th, Stevens RC, Schultz PG, Proc Natl Acad Sci U S A. 2003 Feb 4;100(3):856-61. Epub 2003 Jan 24. PMID:12552112

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