ArticleStructure (London, England : 1993)2018
The Unusual Transmembrane Partition of the Hexameric Channel of the Hepatitis C Virus.
Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- An amphipathic Bax core dimer forms part of the apoptotic pore wall in the mitochondrial␣membrane.The EMBO journal · 2021Article
- Inhibitor Development against p7 Channel in Hepatitis C Virus.Molecules (Basel, Switzerland) · 2021Article
- Membrane Protein Structure Determination and Characterisation by Solution and Solid-State NMR.Biology · 2020Review
- Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein.Nature communications · 2020Article
- Solution NMR: A powerful tool for structural and functional studies of membrane proteins in reconstituted environments.The Journal of biological chemistry · 2019Review
- Article
- Critical Effect of the Detergent:Protein Ratio on the Formation of the Hepatitis C Virus p7 Channel.Biochemistry · 2019Review
- Hepatitis C virus sequence divergence preserves p7 viroporin structural and dynamic features.Scientific reports · 2019Article
- Article
- Chen et al. reply.Nature · 2018Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 3 countries.
Funding
Abstract
The p7 protein of the hepatitis C virus (HCV) can oligomerize in membrane to form cation channels. Previous studies showed that the channel assembly in detergent micelles adopts a unique flower-shaped oligomer, but the unusual architecture also presented problems for understanding how this viroporin resides in the membrane. Moreover, the oligomeric state of p7 remains controversial, as both hexamer and heptamer have been proposed. Here we address the above issues using p7 reconstituted in bicelles that mimic a lipid bilayer. We found, using a recently developed oligomer-labeling method, that p7 forms hexamers in the bicelles. Solvent paramagnetic relaxation enhancement analyses showed that the bilayer thickness around the HCV ion channel is substantially smaller than expected, and thus a significant portion of the previously assigned membrane-embedded region is solvent exposed. Our study provides an effective approach for characterizing the transmembrane partition of small ion channels in near lipid bilayer environment.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.