Prediction of quaternary assembly of SARS coronavirus peplomer.
The tertiary structures of the S1 and S2 domains of the spike protein of the coronavirus which is responsible of the severe acute respiratory syndrome (SARS) have been recently predicted. Here a molecular assembly of SARS coronavirus peplomer which accounts for the available functional data is suggested. The interaction between S1 and S2 appears to be stabilised by a large hydrophobic network of aromatic side chains present in both domains. This feature results to be common to all coronaviruses, suggesting potential targeting for drugs preventing coronavirus-related infections.
Bernini
Andrea
A
Department of Molecular Biology, Biomolecular Structure Research Center, University of Siena, I-53100 Siena, Italy.
Spiga
Ottavia
O
Ciutti
Arianna
A
Chiellini
Stefano
S
Bracci
Luisa
L
Yan
Xiyun
X
Zheng
Bojian
B
Huang
Jiandong
J
He
Ming-Liang
ML
Song
Huai-Dong
HD
Hao
Pei
P
Zhao
Guoping
G
Niccolai
Neri
N
D019943:Amino Acid Substitution; D001665:Binding Sites; D003198:Computer Simulation; D008562:Membrane Glycoproteins / Q000032:analysis / Q000737:chemistry*; D008956:Models, Chemical; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D020539:Sequence Analysis, Protein / Q000379:methods*; D064370:Spike Glycoprotein, Coronavirus; D013329:Structure-Activity Relationship; D014759:Viral Envelope Proteins / Q000032:analysis / Q000737:chemistry*
D008562:Membrane Glycoproteins; D064370:Spike Glycoprotein, Coronavirus; D014759:Viral Envelope Proteins; C578557:spike glycoprotein, SARS-CoV