| Theoretical Model:
The protein structure described on this page was determined theoretically, and hence should be interpreted with caution. |
Model Confidence:
Confident (90 > pLDDT > 70)
AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Some regions below 50 pLDDT may be unstructured in isolation.
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].
Function
Non-structural protein 4 (nsp4)
Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.[2][3]
Non-structural protein 11 (NSP11) is the short peptide at the C-term of the large SARS-CoV-2 polyprotein ORF1ab (pp1a). it is the cleavage product of pp1a polyprotein by 3CLpro/Mpro protease at the nsp10/11 junction. NSP11 overlaps a portion of the RNA that codes for NSP12, so whether NSP11 is actually expressed as well as its putative function is not known[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)
