Dynamics of SARS-coronavirus HR2 domain in the prefusion and transition states.
The envelope glycoproteins S1 and S2 of severe acute respiratory syndrome coronavirus (SARS-CoV) mediate viral entry by conformational change from a prefusion state to a postfusion state that enables fusion of the viral and target membranes. In this work we present the characterization of the dynamic properties of the SARS-CoV S2-HR2 domain (residues 1141-1193 of S) in the prefusion and newly discovered transition states by NMR (15)N relaxation studies. The dynamic properties of the different states, which are stabilized under different experimental conditions, extend the current model of viral membrane fusion and give insight into the design of structure-based antagonists of SARS-CoV in particular, as well as other enveloped viruses such as HIV.
McReynolds
Susanna
S
Department of Biochemistry and Molecular Genetics, College of Medicine, University of Illinois at Chicago, Chicago, IL 60607, USA.
Jiang
Shaokai
S
Rong
Lijun
L
Caffrey
Michael
M
D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D044367:Phase Transition; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D045473:Severe acute respiratory syndrome-related coronavirus / Q000737:chemistry*; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000648:ultrastructure*
D014759:Viral Envelope Proteins