2ghw: Difference between revisions

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{{Seed}}
[[Image:2ghw.png|left|200px]]
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===Crystal structure of SARS spike protein receptor binding domain in complex with a neutralizing antibody, 80R===
===Crystal structure of SARS spike protein receptor binding domain in complex with a neutralizing antibody, 80R===
{{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.


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==About this Structure==
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[[2ghw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Sars_coronavirus Sars coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GHW OCA].
(as it appears on PubMed at http://www.pubmed.gov), where 16954221 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16954221}}


==About this Structure==
==See Also==
2GHW is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Sars_coronavirus Sars coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GHW OCA].
*[[Monoclonal Antibody|Monoclonal Antibody]]


==Reference==
==Reference==
<ref group="xtra">PMID:16954221</ref><references group="xtra"/>
<ref group="xtra">PMID:016954221</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Sars coronavirus]]
[[Category: Sars coronavirus]]
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[[Category: S protein]]
[[Category: S protein]]
[[Category: Sar]]
[[Category: Sar]]
[[Category: Virus/viral protein/antibiotic complex]]
[[Category: Virus-viral protein-antibiotic complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 16:41:03 2009''

Revision as of 08:44, 23 April 2014

Template:STRUCTURE 2ghw

Crystal structure of SARS spike protein receptor binding domain in complex with a neutralizing antibody, 80R

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

2ghw is a 4 chain structure with sequence from Homo sapiens and Sars coronavirus. Full crystallographic information is available from OCA.

See Also

Reference

  1. 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

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