About: The Transmembrane Oligomers of Coronavirus Protein E

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	The Transmembrane Oligomers of Coronavirus Protein E
Creator	Torres, Jaume Parthasarathy, Krupakar Wang, Jifeng Liu, Ding
Source	Elsevier; Medline; PMC
abstract	We have tested the hypothesis that severe acute respiratory syndrome (SARS) coronavirus protein E (SCoVE) and its homologs in other coronaviruses associate through their putative transmembrane domain to form homooligomeric α-helical bundles in vivo. For this purpose, we have analyzed the results of molecular dynamics simulations where all possible conformational and aggregational space was systematically explored. Two main assumptions were considered; the first is that protein E contains one transmembrane α-helical domain, with its N- and C-termini located in opposite faces of the lipid bilayer. The second is that protein E forms the same type of transmembrane oligomer and with identical backbone structure in different coronaviruses. The models arising from the molecular dynamics simulations were tested for evolutionary conservation using 13 coronavirus protein E homologous sequences. It is extremely unlikely that if any of our assumptions were not correct we would find a persistent structure for all the sequences tested. We show that a low energy dimeric, trimeric and two pentameric models appear to be conserved through evolution, and are therefore likely to be present in vivo. In support of this, we have observed only dimeric, trimeric, and pentameric aggregates for the synthetic transmembrane domain of SARS protein E in SDS. The models obtained point to residues essential for protein E oligomerization in the life cycle of the SARS virus, specifically N15. In addition, these results strongly support a general model where transmembrane domains transiently adopt many aggregation states necessary for function.
has issue date	2005-02-01(xsd:dateTime)
bibo:doi	10.1529/biophysj.104.051730
bibo:pmid	15713601
has license	hybrid-oa
sha1sum (hex)	fc9d1baea37339edaa81609ec01500616b8a48b9
schema:url	https://doi.org/10.1529/biophysj.104.051730
resource representing a document's title	The Transmembrane Oligomers of Coronavirus Protein E
has PubMed Central identifier	PMC1305130
has PubMed identifier	15713601
schema:publication	Biophysical Journal
resource representing a document's body	covid:fc9d1baea37339edaa81609ec01500616b8a48b9#body_text
is schema:about of	named entity 'coronavirus' named entity 'identical' named entity 'associate' named entity 'coronaviruses' named entity 'CORONAVIRUS' named entity 'ESSENTIAL' named entity 'IN VIVO' named entity 'LOCATED IN' named entity 'PROTEIN E' named entity 'TRANSMEMBRANE' named entity 'SARS' named entity 'RESULTS' named entity 'SPACE' named entity 'OPPOSITE' named entity 'AGGREGATION' named entity 'TRANSMEMBRANE DOMAIN' named entity 'WHERE' named entity 'LIPID BILAYER' named entity 'ADDITION' named entity 'POSSIBLE' named entity 'CONSIDERED' named entity 'SECOND' named entity 'ASSOCIATE' named entity 'N15' named entity 'APPEAR' named entity 'FORMS' named entity 'THEIR' named entity 'TESTED FOR' named entity 'PROTEIN E' named entity 'EVOLUTIONARY CONSERVATION' named entity 'NECESSARY' named entity 'SAME TYPE' named entity 'SYNTHETIC' named entity 'OBTAINED' named entity 'PURPOSE' named entity 'HAVE' named entity 'ARISING' named entity 'CORRECT' named entity 'BACKBONE' named entity 'CONTAINS' named entity 'HYPOTHESIS' named entity 'SARS VIRUS' named entity 'MAIN' named entity 'TESTED' named entity 'GENERAL' named entity 'LIKELY' named entity 'MOLECULAR DYNAMICS SIMULATIONS' named entity 'MODEL' named entity 'HOMOLOGOUS SEQUENCES' named entity 'THESE' named entity 'EVOLUTION' named entity 'SEQUENCES' named entity 'OLIGOMERS' named entity 'CORONAVIRUSES' named entity 'OLIGOMERIZATION' named entity 'SEVERE ACUTE RESPIRATORY SYNDROME' named entity 'UNLIKELY' named entity 'ANALYZED' named entity 'DOMAIN' named entity 'SUPPORT' named entity 'OUR' named entity 'USING' named entity 'LOW ENERGY' named entity 'OLIGOMER' named entity 'PERSISTENT' named entity 'ADOPT' named entity 'ITS' named entity 'POINT' named entity 'HELICAL' named entity 'FUNCTION' named entity 'IDENTICAL' named entity 'PRESENT' named entity 'EXTREMELY' named entity 'TRANSMEMBRANE' named entity 'CORONAVIRUS' named entity 'STATES' named entity 'TO FORM' named entity 'STRUCTURE'

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