Cargando…
Structure of a Conserved Golgi Complex-targeting Signal in Coronavirus Envelope Proteins
Coronavirus envelope (CoV E) proteins are ∼100-residue polypeptides with at least one channel-forming α-helical transmembrane (TM) domain. The extramembrane C-terminal tail contains a completely conserved proline, at the center of a predicted β-coil-β motif. This hydrophobic motif has been reported...
Autores principales: | Li, Yan, Surya, Wahyu, Claudine, Stephanie, Torres, Jaume |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4007446/ https://www.ncbi.nlm.nih.gov/pubmed/24668816 http://dx.doi.org/10.1074/jbc.M114.560094 |
Ejemplares similares
-
Structural basis of cell-surface signaling by a conserved sigma regulator in Gram-negative bacteria
por: Jensen, Jaime L., et al.
Publicado: (2020) -
Structure of Severe Acute Respiratory Syndrome Coronavirus Receptor-binding Domain Complexed with Neutralizing Antibody
por: Prabakaran, Ponraj, et al.
Publicado: (2006) -
Solution NMR Structure of the Ca(2+)-bound N-terminal Domain of CaBP7: A REGULATOR OF GOLGI TRAFFICKING
por: McCue, Hannah V., et al.
Publicado: (2012) -
Quaternary Structure of Coronavirus Spikes in Complex with Carcinoembryonic Antigen-related Cell Adhesion Molecule Cellular Receptors
por: Lewicki, Daniel N., et al.
Publicado: (2002) -
Crystal Structure of Bovine Coronavirus Spike Protein Lectin Domain
por: Peng, Guiqing, et al.
Publicado: (2012)