2ghv
From Proteopedia
Line 1: | Line 1: | ||
- | {{Seed}} | ||
- | [[Image:2ghv.png|left|200px]] | ||
- | |||
- | <!-- | ||
- | The line below this paragraph, containing "STRUCTURE_2ghv", creates the "Structure Box" on the page. | ||
- | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | ||
- | or leave the SCENE parameter empty for the default display. | ||
- | --> | ||
{{STRUCTURE_2ghv| PDB=2ghv | SCENE= }} | {{STRUCTURE_2ghv| PDB=2ghv | SCENE= }} | ||
- | |||
===Crystal structure of SARS spike protein receptor binding domain=== | ===Crystal structure of SARS spike protein receptor binding domain=== | ||
+ | {{ABSTRACT_PUBMED_16954221}} | ||
- | + | ==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== | ||
- | + | [[2ghv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sars_coronavirus Sars coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GHV OCA]. | |
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:016954221</ref><references group="xtra"/><references/> |
- | [[Category: | + | [[Category: Sars coronavirus]] |
[[Category: Farzan, M.]] | [[Category: Farzan, M.]] | ||
[[Category: Hwang, W C.]] | [[Category: Hwang, W C.]] | ||
Line 36: | Line 23: | ||
[[Category: S protein]] | [[Category: S protein]] | ||
[[Category: Sar]] | [[Category: Sar]] | ||
- | + | [[Category: Viral protein]] | |
- | + |
Revision as of 08:16, 23 April 2014
Contents |
Crystal structure of SARS spike protein receptor binding domain
Template:ABSTRACT PUBMED 16954221
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
2ghv is a 2 chain structure with sequence from Sars coronavirus. Full crystallographic information is available from OCA.
Reference
- Hwang WC, Lin Y, Santelli E, Sui J, Jaroszewski L, Stec B, Farzan M, Marasco WA, Liddington RC. Structural basis of neutralization by a human anti-severe acute respiratory syndrome spike protein antibody, 80R. J Biol Chem. 2006 Nov 10;281(45):34610-6. Epub 2006 Sep 5. PMID:16954221 doi:10.1074/jbc.M603275200
Categories: Sars coronavirus | Farzan, M. | Hwang, W C. | Jaroszewski, L. | Liddington, R C. | Lin, Y. | Marasco, W A. | Santelli, E. | Stec, B. | Sui, J. | S protein | Sar | Viral protein