Cargando…
A trimeric hydrophobic zipper mediates the intramembrane assembly of SARS-CoV-2 spike
The S protein of the SARS-CoV-2 is a Type I membrane protein that mediates membrane fusion and viral entry. A vast amount of structural information is available for the ectodomain of S, a primary target by the host immune system, but much less is known regarding its transmembrane domain (TMD) and it...
Autores principales: | Fu, Qingshan, Chou, James J. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8043453/ https://www.ncbi.nlm.nih.gov/pubmed/33851163 http://dx.doi.org/10.1101/2021.04.09.439203 |
Ejemplares similares
-
Stabilizing the closed SARS-CoV-2 spike trimer
por: Juraszek, Jarek, et al.
Publicado: (2021) -
Intricacies of the SARS-CoV-2 spike transmembrane trimer organization
por: Aliper, Elena T., et al.
Publicado: (2022) -
Identification and application of self-binding zipper-like sequences in SARS-CoV spike protein
por: Zhang, Si Min, et al.
Publicado: (2018) -
Computational and comparative investigation of hydrophobic profile of spike protein of SARS-CoV-2 and SARS-CoV
por: Shekhawat, Uma, et al.
Publicado: (2022) -
An antibody targeting the N-terminal domain of SARS-CoV-2 disrupts the spike trimer
por: Suryadevara, Naveenchandra, et al.
Publicado: (2022)