Sandbox 1k4r
Dengue VirusDengue Virus
| |||||||||
| 1k4r, resolution 24.00Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Related: | 1svb | ||||||||
| |||||||||
| |||||||||
| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Structure of Dengue VirusStructure of Dengue Virus
The first structure of a flavivirus has been determined by using a combination of cryoelectron microscopy and fitting of the known structure of glycoprotein E into the electron density map. The virus core, within a lipid bilayer, has a less-ordered structure than the external, icosahedral scaffold of 90 glycoprotein E dimers. The three E monomers per icosahedral asymmetric unit do not have quasiequivalent symmetric environments. Difference maps indicate the location of the small membrane protein M relative to the overlaying scaffold of E dimers. The structure suggests that flaviviruses, and by analogy also alphaviruses, employ a fusion mechanism in which the distal beta barrels of domain II of the glycoprotein E are inserted into the cellular membrane.
Structure of dengue virus: implications for flavivirus organization, maturation, and fusion., Kuhn RJ, Zhang W, Rossmann MG, Pletnev SV, Corver J, Lenches E, Jones CT, Mukhopadhyay S, Chipman PR, Strauss EG, Baker TS, Strauss JH, Cell. 2002 Mar 8;108(5):717-25. PMID:11893341
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
EtiologyEtiology
Dengue virus is a mosquito borne illness and is a major threat in most of the tropical and sub-tropical countries around the world. There are four related subtypes of the Dengue virus. Dengue is not transmitted directly from person-to-person and symptoms range from a mild fever, to incapacitating high fever, with severe headache, pain behind the eyes, muscle and joint pain, and rash. There is no vaccine or any specific medicine to treat dengue. People who have dengue fever should rest, drink plenty of fluids and reduce the fever using paracetamol or see a doctor.
About this StructureAbout this Structure
Dengue Virus inside Cell
Anything in this section will appear adjacent to the 3D structure and will be scrollable. |
| ||||||||||
Dengue NS5 Protein
The N-terminal domain has the capacity to bind GTP, hold the guanosine of the viral cap structure, and synthesize two different methylation reactions that are required for the formation of the RNA cap (3). A GTP-binding site in the N-terminal domain is suggested to be a cap-binding site for the Dengue-2-methyltransferase (4). The C-terminal subdomain is an RNA-dependent-RNA polymerase (RdRp) domain. The core subunit is responsible for Ado-Met binding and catalytic activity due to the GTP-binding pocket (3). |
| ||||||||||
Dengue NS3/NS2B Protein
The NS3 protease is a serine protease that can also function as a RNA helicase and RTPase/NTPase. The enzymatic function of this protease is important for the Dengue virus to replicate. This enzyme of the virus is also a potential target for vaccines and antiviral drugs. The catalytic triad (His-51, Asp-75 and Ser-135), is found between these two β-barrels, and its activity is dependent on the presence of the . This cofactor wraps around the NS3 protease domain and becomes part of the active site. The NS2B cofactor is critical for proteolytic activation of the NS3 protease. The NS3 protease is made up of an extensive network of hydrogen bond and hydrophobic interaction, making it very rigid. NS2B is also important in contributing to substrate binding. This implies that the NS2B cofactor acts as an enzyme activator as well as being directly involved in substrate binding/interactions. |
| ||||||||||