The concerted conformational changes during human rhinovirus 2 uncoating.

Article Details

Citation

Hewat EA, Neumann E, Blaas D

The concerted conformational changes during human rhinovirus 2 uncoating.

Mol Cell. 2002 Aug;10(2):317-26.

PubMed ID
12191477 [ View in PubMed
]
Abstract

Delivery of the rhinovirus genome into the cytoplasm involves a cooperative structural modification of the viral capsid. We have studied this phenomenon for human rhinovirus serotype 2 (HRV2). The structure of the empty capsid has been determined to a resolution of better than 15 A by cryo-electron microscopy, and the atomic structure of native HRV2 was used to examine conformational changes of the capsid. The two proteins around the 5-fold axes make an iris type of movement to open a 10 A diameter channel which allows the RNA genome to exit, and the N terminus of VP1 exits the capsid at the pseudo 3-fold axis. A remarkable modification occurs at the 2-fold axes where the N-terminal loop of VP2 bends inward, probably to detach the RNA.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Genome polyproteinP04936Details