Structural flexibility of the tetanus neurotoxin revealed by crystallographic and solution scattering analyses

Structural flexibility of the tetanus neurotoxin revealed by crystallographic and solution scattering analyses

Although the tetanus neurotoxin (TeNT) delivers its protease domain (LC) across the synaptic vesicle lumen into the cytosol via its receptor binding domain (HC) and translocation domain (HN), the molecular mechanism coordinating this membrane translocation remains unresolved. Here, we report the hig...

Full description

Bibliographic Details
Main Authors: Chun-ming Zhang, Yoshihiro Imoto, Takaaki Hikima, Tsuyoshi Inoue
Format: Article
Language:English
Published: Elsevier 2021-01-01
Series:Journal of Structural Biology: X
Subjects:
Tetanus neurotoxin
Botulinum neurotoxin
Disulfide bond
Crystallography
Small angle X-ray scattering
Online Access:http://www.sciencedirect.com/science/article/pii/S2590152421000027

Internet

http://www.sciencedirect.com/science/article/pii/S2590152421000027

Similar Items