› 2qj2

X-ray diffraction
1.81Å resolution

A Mechanistic Basis for Converting a Receptor Tyrosine Kinase Agonist to an Antagonist

Released:
DOI: 10.2210/pdb2qj2/pdb
PDB entry 2qj2 coloured by chain, front view.
PDB entry 2qj2 coloured by chain, side view.
PDB entry 2qj2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A mechanistic basis for converting a receptor tyrosine kinase agonist to an antagonist.
Tolbert WD, Daugherty J, Gao C, Xie Q, Miranti C, Gherardi E, Vande Woude G, Xu HE
Proc Natl Acad Sci U S A 104 14592-7 (2007)
PMID: 17804794

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146878 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hepatocyte growth factor alpha chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 184 amino acids
Theoretical weight: 21.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14210 (Residues: 28-209; Coverage: 26%)
Gene names: HGF, HPTA
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: P21
Unit cell:
a: 49.401Å b: 51.805Å c: 73.167Å
α: 90° β: 107.87° γ: 90°
R-values:
R R work R free
0.21 0.201 0.248
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Targeting MET in cancer: rationale and progress.
Gherardi et al. (2012)
8 more

4 mentions without citation

State of the structure address on MET receptor activation by HGF.
Linossi et al. (2021)
3 more