2B6B

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

2B6B の概要

• エントリーDOI: 10.2210/pdb2b6b/pdb
• EMDBエントリー: 1166 1167
• 分子名称: envelope glycoprotein, CD209 antigen (2 entities in total)
• 機能のキーワード: cryo em dengue crd dc-sign, icosahedral virus, virus-receptor complex, virus/receptor
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 151378.20

構造登録者

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. (登録日: 2005-09-30, 公開日: 2006-03-07, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (25 Å)