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-Structure paper
タイトル | Continuous flexibility analysis of SARS-CoV-2 spike prefusion structures. |
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ジャーナル・号・ページ | IUCrJ, Vol. 7, Issue Pt 6, Page 1059-1069, Year 2020 |
掲載日 | 2020年9月29日 |
著者 | Roberto Melero / Carlos Oscar S Sorzano / Brent Foster / José-Luis Vilas / Marta Martínez / Roberto Marabini / Erney Ramírez-Aportela / Ruben Sanchez-Garcia / David Herreros / Laura Del Caño / Patricia Losana / Yunior C Fonseca-Reyna / Pablo Conesa / Daniel Wrapp / Pablo Chacon / Jason S McLellan / Hemant D Tagare / Jose-Maria Carazo / |
PubMed 要旨 | Using a new consensus-based image-processing approach together with principal component analysis, the flexibility and conformational dynamics of the SARS-CoV-2 spike in the prefusion state have been ...Using a new consensus-based image-processing approach together with principal component analysis, the flexibility and conformational dynamics of the SARS-CoV-2 spike in the prefusion state have been analysed. These studies revealed concerted motions involving the receptor-binding domain (RBD), N-terminal domain, and subdomains 1 and 2 around the previously characterized 1-RBD-up state, which have been modeled as elastic deformations. It is shown that in this data set there are not well defined, stable spike conformations, but virtually a continuum of states. An ensemble map was obtained with minimum bias, from which the extremes of the change along the direction of maximal variance were modeled by flexible fitting. The results provide a warning of the potential image-processing classification instability of these complicated data sets, which has a direct impact on the interpretability of the results. |
リンク | IUCrJ / PubMed:33063791 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.9 - 3.3 Å |
構造データ | EMDB-11328, PDB-6zow: EMDB-11336, PDB-6zp5: EMDB-11337, PDB-6zp7: EMDB-11341: |
化合物 | ChemComp-NAG: ChemComp-MAN: ChemComp-DMS: ChemComp-HOH: |
由来 |
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キーワード | VIRAL PROTEIN / Spike / Prefusion / Flexibility / Closed / Open |