有哪些信誉好的足球投注网站crystal structure and functional analysis of the sars-coronavirus rna cap 2′-o-methyltransferase nsp10nsp16 complex晶体结构和功能分析的发热、rna帽2u2032-o-methyltransferase nsp10nsp16复杂.pdfVIP
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crystal structure and functional analysis of the sars-coronavirus rna cap 2′-o-methyltransferase nsp10nsp16 complex晶体结构和功能分析的发热、rna帽2u2032-o-methyltransferase nsp10nsp16复杂
Crystal Structure and Functional Analysis of the SARS- Coronavirus RNA Cap 29-O-Methyltransferase nsp10/ nsp16 Complex 1 1 1 1 1 Etienne Decroly *, Claire Debarnot , Franc¸ois Ferron , Mickael Bouvet , Bruno Coutard , Isabelle 1 1 1 2 ´ 2 Imbert , Laure Gluais , Nicolas Papageorgiou , Andrew Sharff , Gerard Bricogne , Miguel 1 1,3 1 Ortiz-Lombardia , Julien Lescar , Bruno Canard * ´ ´ ´ ´ 1 Centre National de la Recherche Scientifique and Universite de la Mediterranee, UMR 6098, Architecture et Fonction des Macromolecules Biologiques, Marseille, France, 2 Global Phasing Ltd., Sheraton House, Castle Park, Cambridge, United Kingdom, 3 School of Biological Sciences, Nanyang Technological University, Singapore, Republic of Singapore Abstract Cellular and viral S-adenosylmethionine-dependent methyltransferases are involved in many regulated processes such as metabolism, detoxification, signal transduction, chromatin remodeling, nucleic acid processing, and mRNA capping. The Severe Acute Respiratory Syndrome coronavirus nsp16 protein is a S-adenosylmethionine-dependent (nucleoside-29-O)- methyltransferase only active in the presence of its activating partner nsp10. We report the nsp10/nsp16 complex structure ˚ ˚2 at 2.0 A resolution, which shows nsp10 bound to ns
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