About: Crystal structure of the post-fusion core of the Human coronavirus 229E spike protein at 1.86 Å resolution

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About: Crystal structure of the post-fusion core of the Human coronavirus 229E spike protein at 1.86 Å resolution Goto Sponge NotDistinct Permalink

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	Crystal structure of the post-fusion core of the Human coronavirus 229E spike protein at 1.86 Å resolution
Creator	Meng, Bing Xiang, Jiangchao Yan, Lei Yang, Bei Switzerland, Wilson, Ian Hoffmann-La, Roche Ltd, Rudolph, F
Source	Medline; PMC
abstract	Human coronavirus 229E (HCoV-229E) usually causes mild upper respiratory infections in heathy adults, but may lead to severe complications or mortality in individuals with weakened immune systems. Virus entry of HCoV-229E is mediated by its spike (S) protein, where the S1 domain facilitates attachment to host cells and the S2 domain is involved in subsequent fusion of the virus and host membranes. During the fusion process, two heptad repeats, HR1 and HR2, in the S2 domain assemble into a six-helix membrane-fusion structure termed the fusion core. Here, the complete fusion-core structure of HCoV-229E has been determined at 1.86 Å resolution, representing the most complete post-fusion conformation thus far among published human alphacoronavirus (α-HCoV) fusion-core structures. The overall structure of the HCoV-229E fusion core is similar to those of SARS, MERS and HCoV-NL63, but the packing of its 3HR1 core differs from those of SARS and MERS in that it contains more noncanonical ‘x’ and ‘da’ layers. Side-by-side electrostatic surface comparisons reveal that the electrostatic surface potentials are opposite in α-HCoVs and β-HCoVs at certain positions and that the HCoV-229E surface also appears to be the most hydrophobic among the various HCoVs. In addition to the highly conserved hydrophobic interactions between HR1 and HR2, some polar and electrostatic interactions are also well preserved across different HCoVs. This study adds to the structural profiling of HCoVs to aid in the structure-based design of pan-coronavirus small molecules or peptides to inhibit viral fusion.
has issue date	2018-09-03(xsd:dateTime)
bibo:doi	10.1107/s2059798318008318
bibo:pmid	30198895
has license	cc-by
sha1sum (hex)	cb57d1d9d929477c14cabe401b967245c70b4715
schema:url	https://doi.org/10.1107/s2059798318008318
resource representing a document's title	Crystal structure of the post-fusion core of the Human coronavirus 229E spike protein at 1.86 Å resolution
has PubMed Central identifier	PMC6130466
has PubMed identifier	30198895
schema:publication	Acta Crystallogr D Struct Biol
resource representing a document's body	covid:cb57d1d9d929477c14cabe401b967245c70b4715#body_text
is schema:about of	named entity 'fusion' named entity 'conformation' named entity 'HR2' named entity 'upper respiratory infections' named entity 'hydrophobic' named entity 'aid' named entity 'domain' covid:arg/cb57d1d9d929477c14cabe401b967245c70b4715 named entity 'positions' named entity 'surface' named entity 'During' named entity 'electrostatic' named entity 'viral' named entity 'electrostatic interactions' named entity 'MERS' named entity 'inhibit' named entity 'host' named entity 'Crystal structure' named entity 'SARS' named entity 'MERS' named entity 'upper respiratory infections' named entity 'HCoV-229E' named entity 'Human coronavirus 229E' named entity 'coronavirus' named entity 'hydrophobic interactions' named entity 'HCoV-229E' named entity 'Virus entry' named entity 'helix' named entity 'spike protein' named entity 'HCoV-229E' named entity 'solvent-accessible surface area' named entity 'hydrophilic' named entity 'HR1' named entity 'electrostatic' named entity 'proteolytic cleavage' named entity 'hydrophobic' named entity 'NaCl' named entity 'HR2' named entity 'SARS' named entity 'HR1' named entity 'HR1' named entity 'HCoV-NL63' named entity 'HR1' named entity 'highly conserved' named entity 'MERS' named entity 'SARS' named entity 'transmembrane helix' named entity 'd/a' named entity 'helix' named entity 'HR2' named entity 'conformation' named entity 'MERS' named entity 'SARS' named entity 'salt bridges' named entity 'CASTp' named entity 'HCoV-OC43' named entity 'HR2' named entity 'conformation' named entity 'pH 8' named entity 'lysed' named entity 'membrane fusion' named entity 'hydrophobic' named entity 'kDa' named entity 'HR2' named entity 'HCoV-229E' named entity 'polar interactions' named entity 'HCoV-229E' named entity 'HCoV-229E' named entity 'HCoV-NL63' named entity 'HCoV-229E' named entity 'antiparallel' named entity 'amino acids' named entity 'HCoV-NL63'

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