Chung-ke Chang

TL;DR: A SARS-CoV RNP model that conforms to existing data and bears resemblance to the existing RNP structures of RNA viruses is proposed, highlighting the critical role of modular organization and intrinsic disorder of the N protein in the formation and functions of the dynamic RNP capsid in RNA viruses.

TL;DR: This study provides information on the domain structure partition of SARS-CoV N protein and insights into the differing roles of structured and disordered regions in coronavirus nucleocapsid proteins.

TL;DR: The C-terminal domain (CTD) of the SARS-CoV nucleocapsid protein had stronger nucleic acid-binding activity than the NTD, and the crystal structure of the NP248-365 region was solved, suggesting a mechanism for helical RNA packaging in the virus.

TL;DR: The results of this study indicate that N protein has an essential role in the packaging of SARS-CoV RNA.

TL;DR: It is shown that all disordered regions are also capable of binding to RNA, and the important roles of multisite nucleic acid binding and intrinsic disorder in N protein function and RNP packaging are underscore.