📄 Crystallization and preliminary crystallographic analysis of the heptad-repeat complex of SARS coronavirus spike protein

The aetiological agent of an emergent outbreak of atypical pneumonia, severe acute respiratory syndrome (SARS), is a positive-stranded RNA virus (SARS-CoV) belonging to the Coronaviridae family with a genome that differs substantially from those of other known coronaviruses. Highly conserved heptad-repeat (HR1 and HR2) regions in class I viral fusion proteins, including spike protein from SARS coronavirus, interact with each other to form a six-helix bundle, which is called a fusion core. The crystal structure of the fusion core is expected to greatly facilitate drug design. Crystals of the fusion core of SARS-CoV spike protein have been grown at 291 K using PEG 4000 as precipitant. The diffraction pattern of the crystal extends to 2.8 Å resolution at 100 K in-house. The crystals have unit-cell parameters a = 121.2, b = 66.3, c = 70.0 Å, α = γ = 90, β = 107.4° and belong to space group C2. Assuming the presence of six molecules per asymmetric unit, the solvent content is estimated to be about 28%. © 2004 International Union of Crystallography -

keywords 🔗 severe acute (1373) 🔗 fusion core (19) 🔗 spike protein (353) 🔗 six-helix bundle (19) 🔗 etiological agent (62) 🔗 fusion proteins (43) 🔗 drug design (36) 🔗 respiratory syndrome (2004) 🔗 acute respiratory (1734) 🔗 viral fusion (38) 🔗 crystal structure (114)

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