1NGW
Chimeric Affinity Matured Fab 7g12 complexed with mesoporphyrin
Summary for 1NGW
Entry DOI | 10.2210/pdb1ngw/pdb |
Related | 1N7M 3FCT |
Descriptor | Mature Metal Chelatase Catalytic Antibody, Light chain, Mature Metal Chelatase Catalytic Antibody, Heavy chain, N-METHYLMESOPORPHYRIN, ... (4 entities in total) |
Functional Keywords | antibody, immunoglobulin, antigen binding fragment, immune system |
Biological source | Mus musculus, Homo sapiens (house mouse, human) More |
Total number of polymer chains | 4 |
Total formula weight | 94219.61 |
Authors | Yin, J.,Andryski, S.E.,Beuscher IV, A.E.,Stevens, R.C.,Schultz, P.G. (deposition date: 2002-12-18, release date: 2003-02-04, Last modification date: 2024-10-30) |
Primary citation | Yin, J.,Andryski, S.E.,Beuscher IV, A.E.,Stevens, R.C.,Schultz, P.G. Structural evidence for substrate strain in antibody catalysis Proc.Natl.Acad.Sci.USA, 100:856-861, 2003 Cited by PubMed Abstract: 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. PubMed: 12552112DOI: 10.1073/pnas.0235873100 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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