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The structure of the poliovirus 135S cell entry intermediate at 10-angstrom resolution reveals the location of an externalized polypeptide that binds to membranes.

Abstract:

Poliovirus provides a well-characterized system for understanding how nonenveloped viruses enter and infect cells. Upon binding its receptor, poliovirus undergoes an irreversible conformational change to the 135S cell entry intermediate. This transition involves shifts of the capsid protein beta barrels, accompanied by the externalization of VP4 and the N terminus of VP1. Both polypeptides associate with membranes and are postulated to facilitate entry by forming a translocation pore for the ...

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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Filman, DJ More by this author
Steven, AC More by this author
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Journal:
Journal of virology
Volume:
79
Issue:
12
Pages:
7745-7755
Publication date:
2005-06-05
DOI:
EISSN:
1098-5514
ISSN:
0022-538X
URN:
uuid:65cb08a3-4614-408f-956b-db6914ebfc96
Source identifiers:
33115
Local pid:
pubs:33115

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