ArticleProceedings of the National Academy of Sciences of the United States of America2003
Structural evidence for substrate strain in antibody catalysis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Synthesis at the Interface of Chemistry and Biology.Accounts of chemical research · 2024Review
- Selective Recognition of Carbohydrate Antigens by Germline Antibodies Isolated from AID Knockout Mice.Journal of the American Chemical Society · 2022Article
- Structure and Dynamics of Stacking Interactions in an Antibody Binding Site.Biochemistry · 2019Article
- Characterizing the Diversity of the CDR-H3 Loop Conformational Ensembles in Relationship to Antibody Binding Properties.Frontiers in immunology · 2018Article
- Therapeutic Antibodies to Ganglioside GD2 Evolved from Highly Selective Germline Antibodies.Cell reports · 2017Article
- Somatic hypermutation maintains antibody thermodynamic stability during affinity maturation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Diverse specificity and effector function among human antibodies to HIV-1 envelope glycoprotein epitopes exposed by CD4 binding.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Article
- Nickel(II) chelatase variants directly evolved from murine ferrochelatase: porphyrin distortion and kinetic mechanism.Biochemistry · 2011Article
- Synthesis at the interface of chemistry and biology.Journal of the American Chemical Society · 2009Review
- Article
- Porphyrin binding and distortion and substrate specificity in the ferrochelatase reaction: the role of active site residues.Journal of molecular biology · 2008Article
- Modulation of inhibition of ferrochelatase by N-methylprotoporphyrin.The Biochemical journal · 2006Article
- Chelatases: distort to select?Trends in biochemical sciences · 2006Article
- Article
Corrections and comments
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Authors and funding
5 authors.
Funding
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.
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