3g7t
From Proteopedia
Crystal structure of dengue virus type 1 envelope protein in the postfusion conformation
Structural highlights
FunctionQ689G3_9FLAV Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity).[SAAS:SAAS013754_004_099774] Publication Abstract from PubMedDengue virus relies on a conformational change in its envelope protein, E, to fuse the viral lipid membrane with the endosomal membrane and thereby deliver the viral genome into the cytosol. We have determined the crystal structure of a soluble fragment E (sE) of dengue virus type 1 (DEN-1). The protein is in the postfusion conformation even though it was not exposed to a lipid membrane or detergent. At the domain I-domain III interface, 4 polar residues form a tight cluster that is absent in other flaviviral postfusion structures. Two of these residues, His-282 and His-317, are conserved in flaviviruses and are part of the "pH sensor" that triggers the fusogenic conformational change in E, at the reduced pH of the endosome. In the fusion loop, Phe-108 adopts a distinct conformation, forming additional trimer contacts and filling the bowl-shaped concavity observed at the tip of the DEN-2 sE trimer. Crystal structure of dengue virus type 1 envelope protein in the postfusion conformation and its implications for membrane fusion.,Nayak V, Dessau M, Kucera K, Anthony K, Ledizet M, Modis Y J Virol. 2009 May;83(9):4338-44. Epub 2009 Feb 25. PMID:19244332[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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