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2ghw
From Proteopedia
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|PDB= 2ghw |SIZE=350|CAPTION= <scene name='initialview01'>2ghw</scene>, resolution 2.30Å | |PDB= 2ghw |SIZE=350|CAPTION= <scene name='initialview01'>2ghw</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= S ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Human SARS coronavirus]) | |GENE= S ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Human SARS coronavirus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2ghv|2GHV]], [[2ajf|2ajf]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ghw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ghw OCA], [http://www.ebi.ac.uk/pdbsum/2ghw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ghw RCSB]</span> | ||
}} | }} | ||
| Line 32: | Line 35: | ||
[[Category: Stec, B.]] | [[Category: Stec, B.]] | ||
[[Category: Sui, J.]] | [[Category: Sui, J.]] | ||
| - | [[Category: CL]] | ||
[[Category: neutralizing antibody]] | [[Category: neutralizing antibody]] | ||
[[Category: s protein]] | [[Category: s protein]] | ||
[[Category: sar]] | [[Category: sar]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:16:55 2008'' |
Revision as of 00:16, 31 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | S (Human SARS coronavirus) | ||||||
| Related: | 2GHV, 2ajf
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of SARS spike protein receptor binding domain in complex with a neutralizing antibody, 80R
Overview
Severe acute respiratory syndrome (SARS) is a newly emerged infectious disease that caused pandemic spread in 2003. The etiological agent of SARS is a novel coronavirus (SARS-CoV). The coronaviral surface spike protein S is a type I transmembrane glycoprotein that mediates initial host binding via the cell surface receptor angiotensin-converting enzyme 2 (ACE2), as well as the subsequent membrane fusion events required for cell entry. Here we report the crystal structure of the S1 receptor binding domain (RBD) in complex with a neutralizing antibody, 80R, at 2.3 A resolution, as well as the structure of the uncomplexed S1 RBD at 2.2 A resolution. We show that the 80R-binding epitope on the S1 RBD overlaps very closely with the ACE2-binding site, providing a rationale for the strong binding and broad neutralizing ability of the antibody. We provide a structural basis for the differential effects of certain mutations in the spike protein on 80R versus ACE2 binding, including escape mutants, which should facilitate the design of immunotherapeutics to treat a future SARS outbreak. We further show that the RBD of S1 forms dimers via an extensive interface that is disrupted in receptor- and antibody-bound crystal structures, and we propose a role for the dimer in virus stability and infectivity.
About this Structure
2GHW is a Single protein structure of sequence from Homo sapiens and Human sars coronavirus. Full crystallographic information is available from OCA.
Reference
Structural basis of neutralization by a human anti-severe acute respiratory syndrome spike protein antibody, 80R., Hwang WC, Lin Y, Santelli E, Sui J, Jaroszewski L, Stec B, Farzan M, Marasco WA, Liddington RC, J Biol Chem. 2006 Nov 10;281(45):34610-6. Epub 2006 Sep 5. PMID:16954221
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