2B6B

Cryo EM structure of Dengue complexed with CRD of DC-SIGN

Summary for 2B6B

• Entry DOI: 10.2210/pdb2b6b/pdb
• EMDB information: 1166 1167
• Descriptor: envelope glycoprotein, CD209 antigen (2 entities in total)
• Functional Keywords: cryo em dengue crd dc-sign, icosahedral virus, virus-receptor complex, virus/receptor
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 151378.20

Authors

Pokidysheva, E.,Zhang, Y.,Battisti, A.J.,Bator-Kelly, C.M.,Chipman, P.R.,Gregorio, G.,Hendrickson, W.A.,Kuhn, R.J.,Rossmann, M.G. (deposition date: 2005-09-30, release date: 2006-03-07, Last modification date: 2024-02-14)

Primary citation

Pokidysheva, E.,Zhang, Y.,Battisti, A.J.,Bator-Kelly, C.M.,Chipman, P.R.,Xiao, C.,Gregorio, G.,Hendrickson, W.A.,Kuhn, R.J.,Rossmann, M.G.
Cryo-EM reconstruction of dengue virus in complex with the carbohydrate recognition domain of DC-SIGN
Cell(Cambridge,Mass.), 124:485-493, 2006

PubMed Abstract: Dengue virus (DENV) is a significant human pathogen that causes millions of infections and results in about 24,000 deaths each year. Dendritic cell-specific ICAM3 grabbing nonintegrin (DC-SIGN), abundant in immature dendritic cells, was previously reported as being an ancillary receptor interacting with the surface of DENV. The structure of DENV in complex with the carbohydrate recognition domain (CRD) of DC-SIGN was determined by cryo-electron microscopy at 25 A resolution. One CRD monomer was found to bind to two glycosylation sites at Asn67 of two neighboring glycoproteins in each icosahedral asymmetric unit, leaving the third Asn67 residue vacant. The vacancy at the third Asn67 site is a result of the nonequivalence of the glycoprotein environments, leaving space for the primary receptor binding to domain III of E. The use of carbohydrate moieties for receptor binding sites suggests a mechanism for avoiding immune surveillance.

PubMed: 16469696
DOI: 10.1016/j.cell.2005.11.042

Experimental method

ELECTRON MICROSCOPY (25 Å)