2FXP
Solution Structure of the SARS-Coronavirus HR2 Domain
Summary for 2FXP
Entry DOI | 10.2210/pdb2fxp/pdb |
NMR Information | BMRB: 6969 |
Descriptor | Spike glycoprotein (1 entity in total) |
Functional Keywords | prefusion intermediate, trimer, coiled-coil, viral protein |
Biological source | SARS coronavirus |
Cellular location | Virion membrane; Single-pass type I membrane protein: P59594 |
Total number of polymer chains | 3 |
Total formula weight | 18272.15 |
Authors | Caffrey, M.,Hakansson-McReynolds, S.,Jiang, S. (deposition date: 2006-02-06, release date: 2006-03-07, Last modification date: 2024-05-29) |
Primary citation | Hakansson-McReynolds, S.,Jiang, S.,Rong, L.,Caffrey, M. Solution structure of the severe acute respiratory syndrome-coronavirus heptad repeat 2 domain in the prefusion state J.Biol.Chem., 281:11965-11971, 2006 Cited by PubMed Abstract: The envelope glycoprotein, termed the spike protein, of severe acute respiratory syndrome coronavirus (SARS-CoV) is known to mediate viral entry. Similar to other class 1 viral fusion proteins, the heptad repeat regions of SARS-CoV spike are thought to undergo conformational changes from a prefusion form to a subsequent post-fusion form that enables fusion of the viral and host membranes. Recently, the structure of a post-fusion form of SARS-CoV spike, which consists of isolated domains of heptad repeats 1 and 2 (HR1 and HR2), has been determined by x-ray crystallography. To date there is no structural information for the prefusion conformations of SARS-CoV HR1 and HR2. In this work we present the NMR structure of the HR2 domain (residues 1141-1193) from SARS-CoV (termed S2-HR2) in the presence of the co-solvent trifluoroethanol. We find that in the absence of HR1, S2-HR2 forms a coiled coil symmetric trimer with a complex molecular mass of 18 kDa. The S2-HR2 structure, which is the first example of the prefusion form of coronavirus envelope, supports the current model of viral membrane fusion and gives insight into the design of structure-based antagonists of SARS. PubMed: 16507566DOI: 10.1074/jbc.M601174200 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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