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Locked by Design: A Conformationally Constrained Transglutaminase Tag Enables Efficient Site-Specific Conjugation
- Source :
- Angewandte Chemie (International ed. in English). 54(45)
- Publication Year :
- 2015
-
Abstract
- Based on the crystal structure of a natural protein substrate for microbial transglutaminase, an enzyme that catalyzes protein crosslinking, a recognition motif for site-specific conjugation was rationally designed. Conformationally locked by an intramolecular disulfide bond, this structural mimic of a native conjugation site ensured efficient conjugation of a reporter cargo to the therapeutic monoclonal antibody cetuximab without erosion of its binding properties.
- Subjects :
- Models, Molecular
Stereochemistry
Tissue transglutaminase
Protein Conformation
Cetuximab
CHO Cells
Catalysis
Protein structure
Cricetulus
Cell Line, Tumor
Animals
Humans
Disulfides
chemistry.chemical_classification
Bioconjugation
Transglutaminases
biology
Chemistry
Chinese hamster ovary cell
General Chemistry
Protein engineering
biology.organism_classification
Enzyme
Biochemistry
Intramolecular force
biology.protein
Subjects
Details
- ISSN :
- 15213773
- Volume :
- 54
- Issue :
- 45
- Database :
- OpenAIRE
- Journal :
- Angewandte Chemie (International ed. in English)
- Accession number :
- edsair.doi.dedup.....79d91bb7e93c5fa78c2aedd7cd82f61b