1ngy: Difference between revisions

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New page: left|200px<br /> <applet load="1ngy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ngy, resolution 2.20Å" /> '''Chimeric Mature Fab...
 
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[[Image:1ngy.gif|left|200px]]<br />
[[Image:1ngy.gif|left|200px]]<br /><applet load="1ngy" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1ngy" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1ngy, resolution 2.20&Aring;" />
caption="1ngy, resolution 2.20&Aring;" />
'''Chimeric Mature Fab 7g12-Apo'''<br />
'''Chimeric Mature Fab 7g12-Apo'''<br />


==Overview==
==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.
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==
==About this Structure==
1NGY 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NGY OCA].  
1NGY 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=1NGY OCA].  


==Reference==
==Reference==
Line 14: Line 13:
[[Category: Mus musculus, homo sapiens]]
[[Category: Mus musculus, homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Andryski, S.A.]]
[[Category: Andryski, S A.]]
[[Category: Beuscher, A.B.]]
[[Category: Beuscher, A B.]]
[[Category: Schultz, P.G.]]
[[Category: Schultz, P G.]]
[[Category: Stevens, R.C.]]
[[Category: Stevens, R C.]]
[[Category: Yin, J.]]
[[Category: Yin, J.]]
[[Category: antibody]]
[[Category: antibody]]
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[[Category: immunoglobulin]]
[[Category: immunoglobulin]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:38:32 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:05:58 2008''

Revision as of 15:06, 21 February 2008

File:1ngy.gif


1ngy, resolution 2.20Å

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Chimeric Mature Fab 7g12-Apo

OverviewOverview

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 StructureAbout this Structure

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

ReferenceReference

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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