Structural highlights
Function
HVM49_MOUSE
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yin J, Andryski SE, Beuscher AE 4th, Stevens RC, Schultz PG. Structural evidence for substrate strain in antibody catalysis. Proc Natl Acad Sci U S A. 2003 Feb 4;100(3):856-61. Epub 2003 Jan 24. PMID:12552112 doi:10.1073/pnas.0235873100
