To see full content of that page you need the activeISee plugin.
Get the latest version from here.

Structure of IDP00254

Crystal Structure of the Japanese Encephalitis Virus Envelope Protein, strain SA-14-14-2.

Edit deposit information
CSGID target
IDP00254 
PDB Id
3P54 (NCBI MMDB
Authors
V.C.Luca,C.A.Nelson,J.P.Abimansour,M.S.Diamond,D.H.Fremont,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Chris Nelson 
Responsible lab
Washington University 
Deposition Date
Oct 07, 2010 
Release Date
Dec 08, 2010 

Annotation

Description
Viruses of the Flaviviridae family are responsible for causing global health epidemics in humans; diseases ranging from encephalitis to hepatocellular carcinoma. Japanese Encephalitis Virus (JEV) is a leading cause of viral encephalitis. The JEV envelope protein (E) facilitates cellular attachment and membrane fusion. The JEV E protein consists of three domains (domains I, II, and III) that are characteristic of all flavivirus envelopes. In solution, the JEV E protein packs as an antiparallel dimer. However, this dimer interface lacks many contacts observed in other flavivirus E structures. Several neutralizing antibodies that recognize the JEV E protein have been identified. Binding-site mapping reveals that these epitopes fall within the domain I lateral ridge, fusion loop, domain III lateral ridge and domain I-II hinge regions. All regions known to be involved in neutralization of the closely related West Nile virus that also causes encephalitis. The JEV E structure implies that mature JEV virions assemble in a more open conformation than observed for related viruses. The variable spacing between E proteins is a possible mechanism for differential recognition by antibodies and cellular receptors. 
Functional assignment
Neutralizing antibody target  

Ligands

Ligand code Name Ligand type

Structure information

Unit cell parameters

Space Group
I 2 2 2  
Unit Cell

a=61.11Å, b=62.40Å, c=243.04Å
α=90.00, β=90.00, γ=90.00 
Solvent content
53.61  
Matthews coefficient
2.65  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
30.19-2.10Å (2.18-2.10Å)  
Rall(%)
18.1 
Rwork(%)
17.9 (42.7) 
Rfree(%)
22.4 (22.9) 
Num. observed reflections
25663 (2650) 
Num. Rfree reflections
1283 (136) 
Completeness(%)
92.2 (96.9) 

Model parameters

Num Atoms
3045  
Num Waters
210  
Num Hetatoms
0  
Model mean isotropic B factor
54.670Å2  
RMSD bond length
0.009Å  
RMSD bond angle
1.098°  
RMSD dihedral angle
11.732°
 
Filename uploaded
pdb_extract_coord_11333.cif (uploaded on Feb 08, 2011 12:59 PM)  
Inserted
Feb 08, 2011