› 7sz7

Electron Microscopy
3.4Å resolution

Cryo-EM structure of the extracellular module of the full-length EGFR bound to TGF-alpha. "tips-juxtaposed" conformation

Released:
DOI: 10.2210/pdb7sz7/pdb
PDB entry 7sz7 coloured by chain, front view.
PDB entry 7sz7 coloured by chain, side view.
PDB entry 7sz7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A molecular mechanism for the generation of ligand-dependent differential outputs by the epidermal growth factor receptor.
Huang Y, Ognjenovic J, Karandur D, Miller K, Merk A, Subramaniam S, Kuriyan J
Elife 10 (2021)
PMID: 34846302
Related structures: EMD-25563

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132704 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Epidermal growth factor receptor Chains: A, B
Molecule details ›
Chains: A, B
Length: 1210 amino acids
Theoretical weight: 134.43 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P00533 (Residues: 1-1210; Coverage: 100%)
Gene names: EGFR, ERBB, ERBB1, HER1
Sequence domains:
Transforming growth factor alpha Chains: C, D
Molecule details ›
Chains: C, D
Length: 50 amino acids
Theoretical weight: 5.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01135 (Residues: 40-89; Coverage: 37%)
Gene name: TGFA

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.4Å
Relevant EMDB volumes: EMD-25563
Expression systems:
  • Homo sapiens
  • Escherichia coli

Quick links

Citations

4 review citations

ERK1/2-RSK2 Signaling in Regulation of ERĪ±-Mediated Responses.
Lannigan DA. (2022)
3 more

1 mention without citation

Cryo-electron Microscopic Analysis of Single-Pass Transmembrane Receptors.
Cai et al. (2022)