1ZVB: A Structure-Based Mechanism Of Sars Virus Membrane Fusion

Entry of SARS coronavirus into its target cell requires large-scale structural transitions in the viral spike (S) glycoprotein in order to induce fusion of the virus and cell membranes. Here we describe the identification and crystal structures of four distinct alpha-helical domains derived from the highly conserved heptad-repeat (HR) regions of the S2 fusion subunit. The four domains are an antiparallel four-stranded coiled coil, a parallel trimeric coiled coil, a four-helix bundle, and a six-helix bundle that is likely the final fusogenic form of the protein. When considered together, the structural and thermodynamic features of the four domains suggest a possible mechanism whereby the HR regions, initially sequestered in the native S glycoprotein spike, are released and refold sequentially to promote membrane fusion. Our results provide a structural framework for understanding the control of membrane fusion and should guide efforts to intervene in the SARS coronavirus entry process.
PDB ID: 1ZVBDownload
MMDB ID: 38998
PDB Deposition Date: 2005/6/1
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 1.7  Å
Source Organism:
Similar Structures:
Biological Unit for 1ZVB: trimeric; determined by author and by software (PISA)
Molecular Components in 1ZVB
Label Count Molecule
Proteins (3 molecules)
E2 Glycoprotein
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB