3c6e
From Proteopedia
Crystal structure of the precursor membrane protein- envelope protein heterodimer from the dengue 2 virus at neutral pH
Structural highlights
FunctionO11875_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:SAAS026470_004_099774] Publication Abstract from PubMedMany viruses go through a maturation step in the final stages of assembly before being transmitted to another host. The maturation process of flaviviruses is directed by the proteolytic cleavage of the precursor membrane protein (prM), turning inert virus into infectious particles. We have determined the 2.2 angstrom resolution crystal structure of a recombinant protein in which the dengue virus prM is linked to the envelope glycoprotein E. The structure represents the prM-E heterodimer and fits well into the cryo-electron microscopy density of immature virus at neutral pH. The pr peptide beta-barrel structure covers the fusion loop in E, preventing fusion with host cell membranes. The structure provides a basis for identifying the stages of its pH-directed conformational metamorphosis during maturation, ending with release of pr when budding from the host. The flavivirus precursor membrane-envelope protein complex: structure and maturation.,Li L, Lok SM, Yu IM, Zhang Y, Kuhn RJ, Chen J, Rossmann MG Science. 2008 Mar 28;319(5871):1830-4. PMID:18369147[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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