@article {Caieabd4251,
	title = {Distinct conformational states of SARS-CoV-2 spike protein},
	journal = {Science},
	year = {2020},
	publisher = {American Association for the Advancement of Science},
	abstract = {Intervention strategies are urgently needed to control the SARS-CoV-2 (severe acute respiratory syndrome coronavirus 2) pandemic. The trimeric viral spike (S) protein catalyzes fusion between viral and target cell membranes to initiate infection. Here we report two cryo-EM structures, derived from a preparation of the full-length S protein, representing its prefusion (2.9{\r A} resolution) and postfusion (3.0{\r A} resolution) conformations, respectively. The spontaneous transition to the postfusion state is independent of target cells. The prefusion trimer has three receptor-binding domains clamped down by a segment adjacent to the fusion peptide. The postfusion structure is strategically decorated by N-linked glycans, suggesting possible protective roles against host immune responses and harsh external conditions. These findings advance our understanding of SARS-CoV-2 entry and may guide development of vaccines and therapeutics.},
	issn = {0036-8075},
	doi = {10.1126/science.abd4251},
	url = {https://science.sciencemag.org/content/early/2020/07/20/science.abd4251},
	author = {Cai, Yongfei and Zhang, Jun and Xiao, Tianshu and Peng, Hanqin and Sterling, Sarah M. and Walsh, Richard M. and Rawson, Shaun and Rits-Volloch, Sophia and Chen, Bing}
}
