4Q0X

Crystal structure of non-neutralizing antibody in complex with Epitope II of HCV E2

Summary for 4Q0X

• Entry DOI: 10.2210/pdb4q0x/pdb
• Related: 4HZL
• Descriptor: mAb 12 heavy chain, mAb 12 light chain, Envelope glycoprotein E2, ... (4 entities in total)
• Functional Keywords: antibody, anti-hcv e2, hcv e2, immune system-viral protein complex, immune system/viral protein
• Biological source: Mus musculus (mouse); More
• Cellular location: Core protein p21: Host endoplasmic reticulum membrane; Single-pass membrane protein (By similarity). Core protein p19: Virion (By similarity). Envelope glycoprotein E1: Virion membrane; Single-pass type I membrane protein (Potential). Envelope glycoprotein E2: Virion membrane; Single-pass type I membrane protein (Potential). p7: Host endoplasmic reticulum membrane; Multi-pass membrane protein. Protease NS2-3: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein (By similarity). Non-structural protein 4A: Host endoplasmic reticulum membrane; Single-pass type I membrane protein (Potential). Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein. Non-structural protein 5A: Host endoplasmic reticulum membrane; Peripheral membrane protein. RNA-directed RNA polymerase: Host endoplasmic reticulum membrane; Single-pass type I membrane protein (Potential): P27958
• Total number of polymer chains: 3
• Total formula weight: 50579.36

Authors

Deng, L.,Zhang, P. (deposition date: 2014-04-02, release date: 2014-07-09, Last modification date: 2014-08-06)

Primary citation

Deng, L.,Ma, L.,Virata-Theimer, M.L.,Zhong, L.,Yan, H.,Zhao, Z.,Struble, E.,Feinstone, S.,Alter, H.,Zhang, P.
Discrete conformations of epitope II on the hepatitis C virus E2 protein for antibody-mediated neutralization and nonneutralization.
Proc.Natl.Acad.Sci.USA, 111:10690-10695, 2014

PubMed Abstract: The X-ray crystal structure of epitope II on the E2 protein of hepatitis C virus, in complex with nonneutralizing antibody mAb#12, has been solved at 2.90-Å resolution. The spatial arrangement of the essential components of epitope II (ie, the C-terminal α-helix and the N-terminal loop) was found to deviate significantly from that observed in those corresponding complexes with neutralizing antibodies. The distinct conformations are mediated largely by the flexibility of a highly conserved glycine residue that connects these components. Thus, it is the particular tertiary structure of epitope II, which is presented in a spatial and temporal manner, that determines the specificity of antibody recognition and, consequently, the outcome of neutralization or nonneutralization.

PubMed: 25002515
DOI: 10.1073/pnas.1411317111

Experimental method

X-RAY DIFFRACTION (2.9 Å)