6X2A

SARS-CoV-2 u1S2q 1-RBD Up Spike Protein Trimer

Summary for 6X2A

• Entry DOI: 10.2210/pdb6x2a/pdb
• EMDB information: 21997 21999 22000 22001
• Descriptor: Spike glycoprotein (1 entity in total)
• Functional Keywords: trimer, viral protein
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV)
• Total number of polymer chains: 3
• Total formula weight: 422371.36

Authors

Henderson, R.,Acharya, P. (deposition date: 2020-05-20, release date: 2020-05-27, Last modification date: 2024-10-16)

Primary citation

Henderson, R.,Edwards, R.J.,Mansouri, K.,Janowska, K.,Stalls, V.,Gobeil, S.M.C.,Kopp, M.,Li, D.,Parks, R.,Hsu, A.L.,Borgnia, M.J.,Haynes, B.F.,Acharya, P.
Controlling the SARS-CoV-2 spike glycoprotein conformation.
Nat.Struct.Mol.Biol., 27:925-933, 2020

PubMed Abstract: The coronavirus (CoV) spike (S) protein, involved in viral-host cell fusion, is the primary immunogenic target for virus neutralization and the current focus of many vaccine design efforts. The highly flexible S-protein, with its mobile domains, presents a moving target to the immune system. Here, to better understand S-protein mobility, we implemented a structure-based vector analysis of available β-CoV S-protein structures. Despite an overall similarity in domain organization, we found that S-proteins from different β-CoVs display distinct configurations. Based on this analysis, we developed two soluble ectodomain constructs for the SARS-CoV-2 S-protein, in which the highly immunogenic and mobile receptor binding domain (RBD) is either locked in the all-RBDs 'down' position or adopts 'up' state conformations more readily than the wild-type S-protein. These results demonstrate that the conformation of the S-protein can be controlled via rational design and can provide a framework for the development of engineered CoV S-proteins for vaccine applications.

PubMed: 32699321
DOI: 10.1038/s41594-020-0479-4

Experimental method

ELECTRON MICROSCOPY (3.3 Å)