9KMO
HR1 domain from HCoV-OC43 in complex with a pan-CoV inhibitor EK1
Summary for 9KMO
| Entry DOI | 10.2210/pdb9kmo/pdb |
| Descriptor | Spike protein S2' (1 entity in total) |
| Functional Keywords | hr1, ek1, oc43, viral protein |
| Biological source | Human coronavirus OC43 More |
| Total number of polymer chains | 3 |
| Total formula weight | 23107.90 |
| Authors | |
| Primary citation | He, X.,Liu, H.,Yang, G.,Yan, L. Structures of HCoV-OC43 HR1 Domain in Complex with Cognate HR2 or Analogue EK1 Peptide. Viruses, 17:-, 2025 Cited by PubMed Abstract: Human coronavirus OC43 (HCoV-OC43) is usually associated with common colds, but also related to severe disease in the frail. Its envelope glycoproteins spike (S) is responsible for host-cell attachment and membrane fusion. To understand the molecular basis of membrane fusion of HCoV-OC43, we solved the 3.34 Å crystal structure of the post-fusion state formed by two heptad repeat domains (HR1P and HR2P) of OC43-S. This fusion core comprises a parallel trimeric coiled coil of three HR1 helices with 61 Å at length, around which three HR2 helices are entwined in an antiparallel manner, as anticipated. Moreover, a pan-CoV fusion inhibitor EK1 derived from OC43-HR2P was also crystalized with OC43-HR1P in the resolution of 2.71 Å. Parallel comparisons rationalize the design of EK1, maintaining various hydrophobic and charged or hydrophilic interactions formed in the initial fusion core to stabilize the overall conformation. Together, our results not only reveal the critical intrahelical and interhelical interactions underlying the mechanism of action of OC43-S fusion, but also help our understanding on the mechanism of HCoV-OC43 inhibition by analogue HR2 mimic peptide. PubMed: 40143271DOI: 10.3390/v17030343 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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