Cargando…
HECT domain interaction with ubiquitin binding sites on Tsg101-UEV controls HIV-1 egress, maturation, and infectivity
The HECT domain of HECT E3 ligases consists of flexibly linked N- and C-terminal lobes, with a ubiquitin (Ub) donor site on the C-lobe that is directly involved in substrate modification. HECT ligases also possess a secondary Ub binding site in the N-lobe, which is thought to play a role in processi...
Autores principales: | Nyenhuis, David A., Rajasekaran, Rohith, Watanabe, Susan, Strub, Marie-Paule, Khan, Mahfuz, Powell, Michael, Carter, Carol A., Tjandra, Nico |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9944984/ https://www.ncbi.nlm.nih.gov/pubmed/36642186 http://dx.doi.org/10.1016/j.jbc.2023.102901 |
Ejemplares similares
-
Tsg101 chaperone function revealed by HIV-1 assembly inhibitors
por: Strickland, Madeleine, et al.
Publicado: (2017) -
Novel Tsg101 Binding Partners Regulate Viral L Domain Trafficking
por: Strickland, Madeleine, et al.
Publicado: (2021) -
RNA Binding Suppresses Tsg101 Recognition of Ub-Modified Gag and Facilitates Recruitment to the Plasma Membrane
por: Watanabe, Susan M., et al.
Publicado: (2020) -
Cyclic Peptide Inhibitors of the Tsg101 UEV Protein Interactions Refined through Global Docking and Gaussian Accelerated Molecular Dynamics Simulations
por: Lin, Wen-Wei, et al.
Publicado: (2020) -
Hepatitis B virus hijacks TSG101 to facilitate egress via multiple vesicle bodies
por: Zheng, Yingcheng, et al.
Publicado: (2023)