1NGX

Chimeric Germline Fab 7g12 with jeffamine fragment bound

Summary for 1NGX

• Entry DOI: 10.2210/pdb1ngx/pdb
• Related: 1N7M 1NGW 1NGY 1NGZ 3FCT
• Descriptor: Germline Metal Chelatase Catalytic Antibody, Light chain, Germline Metal Chelatase Catalytic Antibody, Heavy chain, O-(O-(2-AMINOPROPYL)-O'-(2-METHOXYETHYL)POLYPROPYLENE GLYCOL 500), ... (4 entities in total)
• Functional Keywords: antibody, immunoglobulin, antigen binding fragment (fab), immune system
• Biological source: Mus musculus, Homo sapiens (house mouse, human); More
• Total number of polymer chains: 4
• Total formula weight: 94083.41

Authors

Yin, J.,Andryski, S.E.,Beuscher, A.B.,Stevens, R.C.,Schultz, P.G. (deposition date: 2002-12-18, release date: 2003-03-18, Last modification date: 2024-11-13)

Primary citation

Yin, J.,Andryski, S.E.,Beuscher, A.B.,Stevens, R.C.,Schultz, P.G.
Structural evidence for substrate strain in antibody catalysis
Proc.Natl.Acad.Sci.USA, 100:856-861, 2003

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: 12552112
DOI: 10.1073/pnas.0235873100

Experimental method

X-RAY DIFFRACTION (1.8 Å)