Cargando…
Intrinsically Unstructured Domain 3 of Hepatitis C Virus NS5A Forms a “Fuzzy Complex” with VAPB-MSP Domain Which Carries ALS-Causing Mutations
Hepatitis C virus (HCV) affects nearly 200 million people worldwide and is a leading factor for serious chronic liver diseases. For replicating HCV genome, the membrane-associated replication machinery needs to be formed by both HCV non-structural proteins including NS5A and human host factors. Rece...
Autores principales: | Gupta, Garvita, Qin, Haina, Song, Jianxing |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3374797/ https://www.ncbi.nlm.nih.gov/pubmed/22720086 http://dx.doi.org/10.1371/journal.pone.0039261 |
Ejemplares similares
-
Structural, Stability, Dynamic and Binding Properties of the ALS-Causing T46I Mutant of the hVAPB MSP Domain as Revealed by NMR and MD Simulations
por: Lua, Shixiong, et al.
Publicado: (2011) -
VAPC, an Human Endogenous Inhibitor for Hepatitis C Virus (HCV) Infection, Is Intrinsically Unstructured but Forms a “Fuzzy Complex” with HCV NS5B
por: Goyal, Shaveta, et al.
Publicado: (2012) -
C-Terminal Auto-Regulatory Motif of Hepatitis C Virus NS5B Interacts with Human VAPB-MSP to Form a Dynamic Replication Complex
por: Gupta, Garvita, et al.
Publicado: (2016) -
NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics
por: Gupta, Garvita, et al.
Publicado: (2015) -
Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranes
por: Qin, Haina, et al.
Publicado: (2014)