1wyy
From Proteopedia
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{{STRUCTURE_1wyy| PDB=1wyy | SCENE= }} | {{STRUCTURE_1wyy| PDB=1wyy | SCENE= }} | ||
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===Post-fusion hairpin conformation of the sars coronavirus spike glycoprotein=== | ===Post-fusion hairpin conformation of the sars coronavirus spike glycoprotein=== | ||
| + | {{ABSTRACT_PUBMED_15840526}} | ||
| - | + | ==Function== | |
| + | [[http://www.uniprot.org/uniprot/SPIKE_CVHSA SPIKE_CVHSA]] S1 attaches the virion to the cell membrane by interacting with human ACE2 and CLEC4M/DC-SIGNR, initiating the infection. Binding to the receptor and internalization of the virus into the endosomes of the host cell probably induces conformational changes in the S glycoprotein. Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes. S2 is a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. | ||
==About this Structure== | ==About this Structure== | ||
| - | [[1wyy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[1wyy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cvhsa Cvhsa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WYY OCA]. |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:015840526</ref><references group="xtra"/> | + | <ref group="xtra">PMID:015840526</ref><references group="xtra"/><references/> |
| - | [[Category: | + | [[Category: Cvhsa]] |
[[Category: Bosch, B J.]] | [[Category: Bosch, B J.]] | ||
[[Category: Duquerroy, S.]] | [[Category: Duquerroy, S.]] | ||
Revision as of 06:49, 23 April 2014
Contents |
Post-fusion hairpin conformation of the sars coronavirus spike glycoprotein
Template:ABSTRACT PUBMED 15840526
Function
[SPIKE_CVHSA] S1 attaches the virion to the cell membrane by interacting with human ACE2 and CLEC4M/DC-SIGNR, initiating the infection. Binding to the receptor and internalization of the virus into the endosomes of the host cell probably induces conformational changes in the S glycoprotein. Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes. S2 is a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes.
About this Structure
1wyy is a 2 chain structure with sequence from Cvhsa. Full crystallographic information is available from OCA.
Reference
- Duquerroy S, Vigouroux A, Rottier PJ, Rey FA, Bosch BJ. Central ions and lateral asparagine/glutamine zippers stabilize the post-fusion hairpin conformation of the SARS coronavirus spike glycoprotein. Virology. 2005 May 10;335(2):276-85. PMID:15840526 doi:10.1016/j.virol.2005.02.022
