1ngw
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(New page: 200px<br /> <applet load="1ngw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ngw, resolution 2.60Å" /> '''Chimeric Affinity M...)
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Revision as of 07:31, 18 November 2007
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Chimeric Affinity Matured Fab 7g12 complexed with mesoporphyrin
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
1NGW is a Single protein structure of sequence from Mus musculus, homo sapiens with MMP as ligand. 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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