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5I08

Prefusion structure of a human coronavirus spike protein

Summary for 5I08
Entry DOI10.2210/pdb5i08/pdb
EMDB information8069
DescriptorSpike glycoprotein,Foldon chimera (1 entity in total)
Functional Keywordscoronavirus, glycoprotein, prefusion, viral protein
Biological sourceHuman coronavirus HKU1 (isolate N5) (HCoV-HKU1)
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Total number of polymer chains3
Total formula weight432887.67
Authors
Kirchdoerfer, R.N.,Cottrell, C.A.,Wang, N.,Pallesen, J.,Yassine, H.M.,Turner, H.L.,Corbett, K.S.,Graham, B.S.,McLellan, J.S.,Ward, A.B. (deposition date: 2016-02-03, release date: 2016-03-02, Last modification date: 2024-11-13)
Primary citationKirchdoerfer, R.N.,Cottrell, C.A.,Wang, N.,Pallesen, J.,Yassine, H.M.,Turner, H.L.,Corbett, K.S.,Graham, B.S.,McLellan, J.S.,Ward, A.B.
Pre-fusion structure of a human coronavirus spike protein.
Nature, 531:118-121, 2016
Cited by
PubMed Abstract: HKU1 is a human betacoronavirus that causes mild yet prevalent respiratory disease, and is related to the zoonotic SARS and MERS betacoronaviruses, which have high fatality rates and pandemic potential. Cell tropism and host range is determined in part by the coronavirus spike (S) protein, which binds cellular receptors and mediates membrane fusion. As the largest known class I fusion protein, its size and extensive glycosylation have hindered structural studies of the full ectodomain, thus preventing a molecular understanding of its function and limiting development of effective interventions. Here we present the 4.0 Å resolution structure of the trimeric HKU1 S protein determined using single-particle cryo-electron microscopy. In the pre-fusion conformation, the receptor-binding subunits, S1, rest above the fusion-mediating subunits, S2, preventing their conformational rearrangement. Surprisingly, the S1 C-terminal domains are interdigitated and form extensive quaternary interactions that occlude surfaces known in other coronaviruses to bind protein receptors. These features, along with the location of the two protease sites known to be important for coronavirus entry, provide a structural basis to support a model of membrane fusion mediated by progressive S protein destabilization through receptor binding and proteolytic cleavage. These studies should also serve as a foundation for the structure-based design of betacoronavirus vaccine immunogens.
PubMed: 26935699
DOI: 10.1038/nature17200
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.04 Å)
Structure validation

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数据于2025-07-16公开中

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