Conjugated protein domains as engineered scaffold proteins
| Autor: | Lenne J M Lemmens, Luc Brunsveld, Christian Ottmann |
|---|---|
| Přispěvatelé: | Chemical Biology, ICMS Core |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Scaffold protein
Scaffold Cell signaling Protein domain Biomedical Engineering Pharmaceutical Science Bioengineering Context (language use) 02 engineering and technology Protein Engineering 01 natural sciences Metabolic engineering Protein Domains Animals Humans Topical Review Pharmacology chemistry.chemical_classification 010405 organic chemistry Organic Chemistry Proteins Hydrogels 021001 nanoscience & nanotechnology Hydrogels/chemistry Conjugated protein 0104 chemical sciences Cell biology chemistry Metabolic Engineering Signal transduction 0210 nano-technology Biotechnology Protein Engineering/methods Proteins/chemistry Signal Transduction |
| Zdroj: | Bioconjugate Chemistry, 31(6), 1596-1603. American Chemical Society Bioconjugate Chemistry |
| ISSN: | 1043-1802 |
| Popis: | Assembly of proteins into higher-order complexes generates specificity and selectivity in cellular signaling. Signaling complex formation is facilitated by scaffold proteins that use modular scaffolding domains, which recruit specific pathway enzymes. Multimerization and recombination of these conjugated native domains allows the generation of, libraries of, engineered multi-domain scaffold proteins. Analysis of these engineered proteins has provided molecular insight into the regulatory mechanism of the native scaffold proteins and the applicability of these synthetic variants. This topical review highlights the use of engineered, conjugated multi-domain scaffold proteins on different length scales in the context of synthetic signaling pathways, metabolic engineering, liquid-liquid phase separation and hydrogel formation. |
| Databáze: | OpenAIRE |
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