4c2i

From Proteopedia

Revision as of 09:50, 19 March 2014

Template:STRUCTURE 4c2i

Cryo-EM structure of Dengue virus serotype 1 complexed with Fab fragments of human antibody 1F4

Template:ABSTRACT PUBMED 24421336

Function

[Q7TGE4_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:SAAS027287_004_099774] [G3F5K5_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]

About this Structure

4c2i is a 10 chain structure with sequence from Dengue virus 1 and Homo sapiens. Full crystallographic information is available from OCA.

See Also

• Antibody

Reference

• Fibriansah G, Tan JL, Smith SA, de Alwis AR, Ng TS, Kostyuchenko VA, Ibarra KD, Wang J, Harris E, de Silva A, Crowe JE Jr, Lok SM. A potent anti-dengue human antibody preferentially recognizes the conformation of E protein monomers assembled on the virus surface. EMBO Mol Med. 2014 Jan 13. PMID:24421336 doi:http://dx.doi.org/10.1002/emmm.201303404