Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion

Hok Kin Choi, Liang Tong, Wladek Minor, Philippe Dumas, Ulrike Boege, Michael G. Rossmann, Gerd Wengler

Research output: Contribution to journalArticlepeer-review

240 Scopus citations

Abstract

Sindbis virus consists of a nucleocapsid core surrounded by a lipid membrane through which penetrate 80 glycoprotein trimers. The structure of the core protein comprising the coat surrounding the genomic RNA has been determined. The poly-peptide fold from residue 114 to residue 264 is homologous to that of chymotrypsin-like serine proteinases with catalytic residues His 141, Asp 163 and Ser 215 of the core protein positioned as in other serine proteinases. The C-terminal tryp-tophan remains in the P1 substrate site subsequent to the autocatalytic cis cleavage of the capsid protein, thus rendering the proteinase inactive. Model building of the Sindbis core protein dimer shows that the nucleocapsid is likely to have TCombining double low line4 quasisymmetry.

Original languageEnglish
Pages (from-to)37-43
Number of pages7
JournalNature
Volume354
Issue number6348
DOIs
StatePublished - 1991
Externally publishedYes

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