2b6b
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(New page: 200px<br /> <applet load="2b6b" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b6b" /> '''Cryo EM structure of Dengue complexed with ...)
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Revision as of 18:52, 12 November 2007
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Cryo EM structure of Dengue complexed with CRD of DC-SIGN
Overview
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.
About this Structure
2B6B is a Protein complex structure of sequences from Dengue virus and Homo sapiens. Full crystallographic information is available from OCA.
Reference
Cryo-EM reconstruction of dengue virus in complex with the carbohydrate recognition domain of DC-SIGN., Pokidysheva E, Zhang Y, Battisti AJ, Bator-Kelly CM, Chipman PR, Xiao C, Gregorio GG, Hendrickson WA, Kuhn RJ, Rossmann MG, Cell. 2006 Feb 10;124(3):485-93. PMID:16469696
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