Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 57, Issue 44, Pages 14350-14361Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201805869
Keywords
crosslinking; genetic code expansion; unnatural amino acids; protein-protein interactions; proximity-triggered reactions
Categories
Funding
- Excellence Initiative Marie Curie COFUND Program
- EU Marie Curie COFUND Program
- Excellence Cluster CIPSM
- DFG [SFB1035, GRK1721, SPP1623]
- Fonds der Chemischen Industrie (Kekule Fellowship)
Ask authors/readers for more resources
Protein-protein interactions are central to many biological processes. A considerable challenge consists however in understanding and deciphering when and how proteins interact, and this can be particularly difficult when interactions are weak and transient. The site-specific incorporation of unnatural amino acids (UAAs) that crosslink with nearby molecules in response to light provides a powerful tool for mapping transient protein-protein interactions and for defining the structure and topology of protein complexes both invitro and invivo. Complementary strategies consist in site-specific incorporation of UAAs bearing electrophilic moieties that react with natural nucleophilic amino acids in a proximity-dependent manner, thereby chemically stabilizing low-affinity interactions and providing additional constraints on distances and geometries in protein complexes. Herein, we review how UAAs bearing fine-tuned chemical moieties that react with proteins in their vicinity can be utilized to map, study, and characterize weak and transient protein-protein interactions in living systems.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available