Structure and topology around the cleavage site regulate post-translational cleavage of the HIV-1 gp160 signal peptide

Structure and topology around the cleavage site regulate post-translational cleavage of the HIV-1 gp160 signal peptide

Like all other secretory proteins, the HIV-1 envelope glycoprotein gp160 is targeted to the endoplasmic reticulum (ER) by its signal peptide during synthesis. Proper gp160 folding in the ER requires core glycosylation, disulfide-bond formation and proline isomerization. Signal-peptide cleavage occur...

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Bibliographic Details
Main Authors: Erik Lee Snapp, Nicholas McCaul, Matthias Quandte, Zuzana Cabartova, Ilja Bontjer, Carolina Källgren, IngMarie Nilsson, Aafke Land, Gunnar von Heijne, Rogier W Sanders, Ineke Braakman
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2017-07-01
Series:eLife
Subjects:
signal peptide
translocation
endoplasmic reticulum
HIV
gp160
protein folding
Online Access:https://elifesciences.org/articles/26067

Internet

https://elifesciences.org/articles/26067

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