期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 60, 期 16, 页码 8678-8682出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202013193
关键词
actin filaments; drug design; electron microscopy; photoswitch; protein structures
资金
- Max Planck Society
- state of Thuringia [43-5572-321-12040-12]
- European Research Council under the European Union [615984]
- DAAD predoctoral fellowship
- EMBO long-term fellowship
- Projekt DEAL
- Studienstiftung des deutschen Volkes
This study presents the structures of a cell-permeable optojasp bound to actin filaments and highlights the effects of photoswitching a functionalized azobenzene for the first time. Analyzing the binding site and conformational changes within F-actin dependent on the optojasp isomeric state refines the determinants for designing functional F-actin photoswitches.
Actin is essential for key processes in all eukaryotic cells. Cellpermeable optojasps provide spatiotemporal control of the actin cytoskeleton, confining toxicity and potentially rendering F-actin druggable by photopharmacology. Here, we report cryo electron microscopy (cryo-EM) structures of both isomeric states of one optojasp bound to actin filaments. The high-resolution structures reveal for the first time the pronounced effects of photoswitching a functionalized azobenzene. By characterizing the optojasp binding site and identifying conformational changes within F-actin that depend on the optojasp isomeric state, we refine determinants for the design of functional F-actin photoswitches.
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