Structure of the Membrane Anchor of Pestivirus Glycoprotein Erns, a Long Tilted Amphipathic Helix
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چکیده
منابع مشابه
Structure of the Membrane Anchor of Pestivirus Glycoprotein Erns, a Long Tilted Amphipathic Helix
E(rns) is an essential virion glycoprotein with RNase activity that suppresses host cellular innate immune responses upon being partially secreted from the infected cells. Its unusual C-terminus plays multiple roles, as the amphiphilic helix acts as a membrane anchor, as a signal peptidase cleavage site, and as a retention/secretion signal. We analyzed the structure and membrane binding propert...
متن کاملLipid Binding of the Amphipathic Helix Serving as Membrane Anchor of Pestivirus Glycoprotein Erns
Pestiviruses express a peculiar protein named Erns representing envelope glycoprotein and RNase, which is important for control of the innate immune response and persistent infection. The latter functions are connected with secretion of a certain amount of Erns from the infected cell. Retention/secretion of Erns is most likely controlled by its unusual membrane anchor, a long amphipathic helix ...
متن کاملThe pestivirus glycoprotein Erns is anchored in plane in the membrane via an amphipathic helix.
E(rns) is a structural glycoprotein of pestiviruses found to be attached to the virion and to membranes within infected cells via its COOH terminus, although it lacks a hydrophobic anchor sequence. The COOH-terminal sequence was hypothesized to fold into an amphipathic alpha-helix. Alanine insertion scanning revealed that the ability of the E(rns) COOH terminus to bind membranes is considerably...
متن کاملThe Pestivirus Glycoprotein E Is Anchored in Plane in the Membrane via an Amphipathic Helix*
Erns is a structural glycoprotein of pestiviruses found to be attached to the virion and tomembraneswithin infected cells via its COOH terminus, although it lacks a hydrophobic anchor sequence. The COOH-terminal sequence was hypothesized to fold into an amphipathic -helix. Alanine insertion scanning revealed that the ability of the Erns COOH terminus to bind membranes is considerably reduced by...
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ژورنال
عنوان ژورنال: PLoS Pathogens
سال: 2014
ISSN: 1553-7374
DOI: 10.1371/journal.ppat.1003973