› 4hrn

X-ray diffraction
2.65Å resolution

Structural Basis for Eliciting a Cytotoxic Effect in HER2-Overexpressing Cancer Cells via Binding to the Extracellular Domain of HER2

Released:
DOI: 10.2210/pdb4hrn/pdb
PDB entry 4hrn coloured by chain, front view.
PDB entry 4hrn coloured by chain, side view.
PDB entry 4hrn coloured by chain, top view.
Source organisms:
Primary publication:
Structural basis for eliciting a cytotoxic effect in HER2-overexpressing cancer cells via binding to the extracellular domain of HER2.
Jost C, Schilling J, Tamaskovic R, Schwill M, Honegger A, Plückthun A
Structure 21 1979-91 (2013)
PMID: 24095059

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
hetero tetramer
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138067 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Designed Ankyrin Repeat Protein H10-2-G Chains: A, B
Molecule details ›
Chains: A, B
Length: 136 amino acids
Theoretical weight: 14.62 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
Structure domains: Ankyrin repeat-containing domain
Receptor tyrosine-protein kinase erbB-2 Chains: C, D
Molecule details ›
Chains: C, D
Length: 103 amino acids
Theoretical weight: 11.66 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P04626 (Residues: 529-625; Coverage: 8%)
Gene names: ERBB2, HER2, MLN19, NEU, NGL
Sequence domains: Growth factor receptor domain IV
Structure domains: Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: R32
Unit cell:
a: 195Å b: 195Å c: 112Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.219 0.218 0.249
Expression systems:
  • Escherichia coli
  • Spodoptera frugiperda

Quick links

Citations

8 review citations

Designed ankyrin repeat proteins (DARPins): binding proteins for research, diagnostics, and therapy.
Plückthun A. (2015)
7 more

8 mentions without citation

Designer Oncolytic Adenovirus: Coming of Age.
Baker et al. (2018)
7 more