Description
Metadata
Settings
About:
Abstract The membrane anchors of viral envelope proteins play essential roles in cell entry. Recent crystal structures of the ectodomain of envelope protein E2 from a pestivirus suggest that E2 belongs to a novel structural class of membrane fusion machinery. Based on geometric constraints from the E2 structures, we generated atomic models of the E1 and E2 membrane anchors using computational approaches. The E1 anchor contains two amphipathic perimembrane helices and one transmembrane helix; the E2 anchor contains a short helical hairpin stabilized in the membrane by an arginine residue, similar to flaviviruses. A pair of histidine residues in the E2 ectodomain may participate in pH sensing. The proposed atomic models point to Cys987 in E2 as the site of disulfide bond linkage with E1 to form E1–E2 heterodimers. The membrane anchor models provide structural constraints for the disulfide bonding pattern and overall backbone conformation of the E1 ectodomain.
Permalink
an Entity references as follows:
Subject of Sentences In Document
Object of Sentences In Document
Explicit Coreferences
Implicit Coreferences
Graph IRI
Count
http://ns.inria.fr/covid19/graph/entityfishing
4
http://ns.inria.fr/covid19/graph/articles
3
Faceted Search & Find service v1.13.91
Alternative Linked Data Documents:
Sponger
|
ODE
Raw Data in:
CXML
|
CSV
| RDF (
N-Triples
N3/Turtle
JSON
XML
) | OData (
Atom
JSON
) | Microdata (
JSON
HTML
) |
JSON-LD
About
This work is licensed under a
Creative Commons Attribution-Share Alike 3.0 Unported License
.
OpenLink Virtuoso
version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Copyright © 2009-2025 OpenLink Software