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4JZO

Three dimensional structure of broadly neutralizing human anti - Hepatitis C virus (HCV) glycoprotein E2 Fab fragment HC84-27

Summary for 4JZO
Entry DOI10.2210/pdb4jzo/pdb
Related4JZN
DescriptorAnti-HCV E2 Fab HC84-27 heavy chain, Anti-HCV E2 Fab HC84-27 light chain, Envelope glycoprotein E2, ... (4 entities in total)
Functional Keywordsfab fragment, immunglobulin fold, antibody, immune system-viral protein complex, immune system/viral protein
Biological sourceHomo sapiens (human)
More
Cellular locationCore 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 chains12
Total formula weight209724.16
Authors
Krey, T.,Rey, F.A. (deposition date: 2013-04-03, release date: 2013-06-05, Last modification date: 2023-09-20)
Primary citationKrey, T.,Meola, A.,Keck, Z.Y.,Damier-Piolle, L.,Foung, S.K.,Rey, F.A.
Structural basis of HCV neutralization by human monoclonal antibodies resistant to viral neutralization escape.
Plos Pathog., 9:e1003364-e1003364, 2013
Cited by
PubMed: 23696737
DOI: 10.1371/journal.ppat.1003364
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.22 Å)
Structure validation

219140

数据于2024-05-01公开中

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