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| {{STRUCTURE_1zvb| PDB=1zvb | SCENE= }} | | {{STRUCTURE_1zvb| PDB=1zvb | SCENE= }} |
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| '''A structure-based mechanism of SARS virus membrane fusion'''
| | ===A structure-based mechanism of SARS virus membrane fusion=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16698550}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16698550 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16698550}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Sars coronavirus]] | | [[Category: Sars coronavirus]] |
| [[Category: Virus entry]] | | [[Category: Virus entry]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:07:02 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:59:36 2008'' |