› 3j7g

Electron Microscopy
13.6Å resolution

Electron cryo-microscopy of human papillomavirus 16 and H16.V5 Fab fragments

Released:
DOI: 10.2210/pdb3j7g/pdb
PDB entry 3j7g coloured by chain, front view.
PDB entry 3j7g coloured by chain, side view.
PDB entry 3j7g coloured by chain, top view.
Source organism: Human papillomavirus type 16
Primary publication:
A cryo-electron microscopy study identifies the complete H16.V5 epitope and reveals global conformational changes initiated by binding of the neutralizing antibody fragment.
Lee H, Brendle SA, Bywaters SM, Guan J, Ashley RE, Yoder JD, Makhov AM, Conway JF, Christensen ND, Hafenstein S
J Virol 89 1428-38 (2015)
PMID: 25392224
Related structures: EMD-5994

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo 300-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136567 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major capsid protein L1 Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 455 amino acids
Theoretical weight: 50.87 KDa
Source organism: Human papillomavirus type 16
UniProt:
  • Canonical: P03101 (Residues: 21-474; Coverage: 90%)
Gene name: L1
Sequence domains: L1 (late) protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 13.6Å
Relevant EMDB volumes: EMD-5994

Quick links

Citations

6 review citations

Self-assembling protein nanoparticles in the design of vaccines.
López-Sagaseta et al. (2016)
5 more

1 mention without citation

A cryo-electron microscopy study identifies the complete H16.V5 epitope and reveals global conformational changes initiated by binding of the neutralizing antibody fragment.
Lee et al. (2015)