SARS-CoV-2 protein NSP4

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

To the right is an AlphaFold2 3D model of SARS CoV-2 Protein NSP4 (length = 500 amino acids, i.e. YP_009725300.1, color coded by the pLDDT scores. It corresponds to the highest ranked model in terms of the pLDDT confidence scores, i.e., model 1^[1].

Morph of the top 5 ranked AlphaFold2 models of SARS-CoV-2 Protein NSP4, rainbow color coded N-C (blue to red)^[1].

Function

Non-structural protein 4 (nsp4) Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.^[2][3][4].

Structural Highlights

Giri's lab^[5] studied NSP11 in solution and by molecular dynamics. Based on CD, they found that NSP11 shows characteristics of an intrinsically disordered protein (IDP). They further studied the its conformational behavior in the presence of negatively charged and neutral liposomes, and found that it remains disordered. However, in SDS micelle, NSP11 adopts an α-helical conformation, suggesting the helical propensity of NSP11, which is very similar to what [AlphaFold[2 predicts. Based on MD simulations NSP11 appears to to have the behavior of an IDP.

See also

Coronavirus_Disease 2019 (COVID-19)