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A ligand-binding pocket in the dengue virus envelope glycoprotein.

Modis Y, Ogata S, Clements D, Harrison SC
Proc Natl Acad Sci U S A 100 6986-91 (2003)
Related entries: 1oke, 1svb

Cited: 669 times
EuropePMC logo PMID: 12759475

Abstract

Dengue virus is an emerging global health threat. Its major envelope glycoprotein, E, mediates viral attachment and entry by membrane fusion. A crystal structure of the soluble ectodomain of E from dengue virus type 2 reveals a hydrophobic pocket lined by residues that influence the pH threshold for fusion. The pocket, which accepts a hydrophobic ligand, opens and closes through a conformational shift in a beta-hairpin at the interface between two domains. These features point to a structural pathway for the fusion-activating transition and suggest a strategy for finding small-molecule inhibitors of dengue and other flaviviruses.

Reviews - 1oan mentioned but not cited (14)

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Articles - 1oan mentioned but not cited (93)

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Reviews citing this publication (117)

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  1. The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution.. Rey FA, Heinz FX, Mandl C, Kunz C, Harrison SC Nature 375 291-8 (1995)

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