2ghw
From Proteopedia
m (Protected "2ghw" [edit=sysop:move=sysop]) |
Revision as of 08:44, 23 April 2014
Contents |
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
- 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
