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Hepatitis C virus sequence divergence preserves p7 viroporin structural and dynamic features

Abstract:

The hepatitis C virus (HCV) viroporin p7 oligomerizes to form ion channels, which are required for the assembly and secretion of infectious viruses. The 63-amino acid p7 monomer has two putative transmembrane domains connected by a cytosolic loop, and has both N- and C- termini exposed to the endoplasmic reticulum (ER) lumen. NMR studies have indicated differences between p7 structures of distantly related HCV genotypes. A critical question is whether these differences arise from the high seq...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's Version

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Publisher copy:
10.1038/s41598-019-44413-x

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More from this funder
Funding agency for:
Schnell, JR
Oxford Glycobiology Endowment More from this funder
Publisher:
Springer Nature Publisher's website
Journal:
Scientific Reports Journal website
Volume:
9
Issue:
1
Pages:
Article: 8383
Publication date:
2019-06-10
Acceptance date:
2019-05-10
DOI:
EISSN:
2045-2322
Pubs id:
pubs:997782
URN:
uri:52de8ea1-b6d5-4aec-8e50-6ded26fec211
UUID:
uuid:52de8ea1-b6d5-4aec-8e50-6ded26fec211
Local pid:
pubs:997782

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