PDBsum entry 6x2c

Viral protein

PDB id: 6x2c

Contents

Protein chains

971 a.a.

PDB id:

6x2c

Name:

Viral protein

Title:

Sars-cov-2 u1s2q all down rbd state spike protein trimer

Structure:

Spike glycoprotein. Chain: a, b, c. Fragment: ectodomain (unp residues 16-1208). Synonym: s glycoprotein,e2,peplomer protein. Engineered: yes. Mutation: yes

Source:

Severe acute respiratory syndrome coronavirus 2. 2019-ncov. Organism_taxid: 2697049. Gene: s, 2. Expressed in: homo sapiens. Expression_system_taxid: 9606

Authors:

R.Henderson,P.Acharya

Key ref:

R.Henderson et al. (2020). Controlling the SARS-CoV-2 spike glycoprotein conformation. Nat Struct Mol Biol, 27, 925-933. PubMed id: 32699321

Date:

20-May-20 Release date: 27-May-20

Protein chains

P0DTC2  (SPIKE_SARS2) -  Spike glycoprotein from Severe acute respiratory syndrome coronavirus 2

Seq: 1273 a.a.

Struc: 971 a.a.*

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

Nat Struct Mol Biol 27:925-933 (2020)

PubMed id: 32699321

Controlling the SARS-CoV-2 spike glycoprotein conformation.

R.Henderson, R.J.Edwards, K.Mansouri, K.Janowska, V.Stalls, S.M.C.Gobeil, M.Kopp, D.Li, R.Parks, A.L.Hsu, M.J.Borgnia, B.F.Haynes, P.Acharya.

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.