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Role of Salt Bridge Formation in Antigen-Antibody Interaction
- Source :
- Journal of Biological Chemistry. 271:32612-32616
- Publication Year :
- 1996
- Publisher :
- Elsevier BV, 1996.
-
Abstract
- For elucidation of the role of salt bridge formation in the antigen-antibody complex, the interaction between hen egg white lysozyme (HEL) and its monoclonal antibody HyHEL10, the structure of which has been well characterized and forms one salt bridge (Lys97 of HEL and Asp32 of HyHEL10 heavy chain variable region (VH)), was investigated. Asp32 of VH was substituted with Ala, Asn, or Glu by site-directed mutagenesis, and the interaction between HEL and the mutant fragments of the variable region of light chain was investigated by inhibition of the enzymatic activity of HEL and isothermal titration calorimetry. Inhibition assay indicated that these mutations lowered the inhibition only slightly. Thermodynamic study indicated that the negative enthalpic change in the interaction between each of the mutant variable regions of light chain and HEL was significantly increased, although the association constant was slightly decreased, suggesting that these mutations increased the entropy change upon antigen-antibody binding. These results indicate that the role of salt bridge formation in the HyHEL10-HEL interaction is to lower the entropic loss due to binding. In the mutant proteins, the numbers of residues that were perturbed structurally on binding increased, suggesting that the salt bridge suppresses excess structural movement of the antibody upon binding.
- Subjects :
- chemistry.chemical_classification
biology
medicine.drug_class
Mutant
chemical and pharmacologic phenomena
Isothermal titration calorimetry
Cell Biology
Monoclonal antibody
Immunoglobulin light chain
Biochemistry
Antigen-antibody interaction
chemistry.chemical_compound
Enzyme
chemistry
medicine
biology.protein
Lysozyme
Antibody
Molecular Biology
Subjects
Details
- ISSN :
- 00219258
- Volume :
- 271
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry
- Accession number :
- edsair.doi...........5c89fded58a27de3425c55a17d417124
- Full Text :
- https://doi.org/10.1074/jbc.271.51.32612