› 3j7e

Electron Microscopy
13.6Å resolution

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

Released:
DOI: 10.2210/pdb3j7e/pdb
PDB entry 3j7e coloured by chain, front view.
PDB entry 3j7e coloured by chain, side view.
PDB entry 3j7e coloured by chain, top view.
Source organism: Mus musculus
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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero 480-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-207946 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
H16.V5 Fab light chain Chains: A, C, E, L
Molecule details ›
Chains: A, C, E, L
Length: 115 amino acids
Theoretical weight: 12.62 KDa
Source organism: Mus musculus
Ig-like domain-containing protein Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 121 amino acids
Theoretical weight: 13.5 KDa
Source organism: Mus musculus
UniProt:
  • Canonical: K7TH34 (Residues: 1-91, 92-110; Coverage: 99%)
Sequence domains: Immunoglobulin V-set domain

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

2 mentions 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)
1 more