Zala Živič (Avtor), Žiga Strmšek (Avtor), Marko Novinec (Avtor), Jurij Lah (Avtor), San Hadži (Avtor)

Povzetek

Spike trimer plays a key role in SARS-CoV-2 infection and vaccine development. It consists of a globular head and a flexible stalk domain that anchors the protein into the viral membrane. While the head domain has been extensively studied, the properties of the adjoining stalk are poorly understood. Here, we characterize the coiled-coil formation and thermodynamic stability of the stalk domain and its segments. We find that the N-terminal segment of the stalk does not form coiled-coils and remains disordered in solution. The C-terminal stalk segment forms a trimeric coiled-coil in solution, which becomes significantly stabilized in the context of the full-length stalk. Its crystal structure reveals a novel antiparallel tetramer coiled-coil with an unusual combination of a-d and e-a-d hydrophobic core packing. Structural analysis shows that a subset of hydrophobic residues stabilizes different coiled-coil structures: trimer, tetramer, and heterohexamer, underscoring a highly polymorphic nature of the SARS-CoV-2 stalk sequence.

Ključne besede

protein spike;korona virus;obvita vijačnica;spike protein;corona virus;coiled-coil;

Podatki

Jezik: Angleški jezik
Leto izida:
Tipologija: 1.01 - Izvirni znanstveni članek
Organizacija: UL FKKT - Fakulteta za kemijo in kemijsko tehnologijo
UDK: 577.322
COBISS: 97817859 Povezava se bo odprla v novem oknu
ISSN: 0892-6638
Št. ogledov: 105
Št. prenosov: 33
Ocena: 0 (0 glasov)
Metapodatki: JSON JSON-RDF JSON-LD TURTLE N-TRIPLES XML RDFA MICRODATA DC-XML DC-RDF RDF

Ostali podatki

Sekundarni jezik: Slovenski jezik
Sekundarne ključne besede: SARS-CoV-2 (virus);
Vrsta dela (COBISS): Članek v reviji
Strani: str. 1-11
Letnik: ǂVol. ǂ36
Zvezek: ǂiss. ǂ3
Čas izdaje: Mar. 2022
DOI: 10.1096/fj.202101670R
ID: 15437279