Mukherjee, Shruti
Bhattacharyya, Dipita
Bhunia, Anirban
2020-08-19T15:22:57Z
2020-08-19T15:22:57Z
2020
0301-4622
https://doi.org/10.1016/j.bpc.2020.106452
http://hdl.handle.net/20.500.12010/11964
he Envelope (E) protein in SARS Coronavirus (CoV) is a small structural protein, incorporated as part of
the envelope. A major fraction of the protein has been known to be associated with the host membranes,
particularly organelles related to intracellular trafficking, prompting CoV packaging and propagation. Studies
have elucidated the central hydrophobic transmembrane domain of the E protein being responsible for much of
the viroporin activity in favor of the virus. However, newer insights into the organizational principles at the
membranous compartments within the host cells suggest further complexity of the system. The lesser
hydrophobic Carboxylic-terminal of the protein harbors interesting amino acid sequences- suggesting at the
prevalence of membrane-directed amyloidogenic properties that remains mostly elusive. These highly conserved
segments indicate at several potential membrane-associated functional roles that can redefine our comprehensive
understanding of the protein. This should prompt further studies in designing and characterizing of effective
targeted therapeutic measure
30 páginas
image/jepg
Biophysical Chemistry
reponame:Expeditio Repositorio Institucional UJTL
instname:Universidad de Bogotá Jorge Tadeo Lozano
SARS CoV
E protein
Membrane
Structure
Covid-19
Amyloidogenesis
Host-membrane interacting interface of the SARS coronavirus envelope protein: Immense functional potential of C-terminal domain
Artículo
Síndrome respiratorio agudo grave
COVID-19
SARS-CoV-2
Coronavirus
info:eu-repo/semantics/embargoedAccess
info:eu-repo/semantics/acceptedVersion
Acceso restringido
https://doi.org/10.1016/j.bpc.2020.106452