› 5tx4

X-ray diffraction
1.88Å resolution

Derivative of mouse TGF-beta2, with a deletion of residues 52-71 and K25R, R26K, L51R, A74K, C77S, L89V, I92V, K94R T95K, I98V single amino acid substitutions, bound to human TGF-beta type II receptor ectodomain residues 15-130

Released:
DOI: 10.2210/pdb5tx4/pdb
PDB entry 5tx4 coloured by chain, front view.
PDB entry 5tx4 coloured by chain, side view.
PDB entry 5tx4 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
An engineered transforming growth factor β (TGF-β) monomer that functions as a dominant negative to block TGF-β signaling.
Kim SK, Barron L, Hinck CS, Petrunak EM, Cano KE, Thangirala A, Iskra B, Brothers M, Vonberg M, Leal B, Richter B, Kodali R, Taylor AB, Du S, Barnes CO, Sulea T, Calero G, Hart PJ, Hart MJ, Demeler B, Hinck AP
J Biol Chem 292 7173-7188 (2017)
PMID: 28228478

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153364 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
TGF-beta receptor type-2 Chain: A
Molecule details ›
Chain: A
Length: 116 amino acids
Theoretical weight: 13.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P37173 (Residues: 38-153; Coverage: 21%)
Gene name: TGFBR2
Sequence domains: Transforming growth factor beta receptor 2 ectodomain
Structure domains: CD59
Transforming growth factor beta-2 Chain: B
Molecule details ›
Chain: B
Length: 92 amino acids
Theoretical weight: 10.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P61812 (Residues: 303-414; Coverage: 23%)
Gene name: TGFB2
Sequence domains: Transforming growth factor beta like domain
Structure domains: Cystine-knot cytokines

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 39.019Å b: 70.772Å c: 77.116Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.194 0.222
Expression system: Escherichia coli

Quick links

Citations

4 review citations

TGFβ biology in cancer progression and immunotherapy.
Derynck et al. (2021)
3 more

3 mentions without citation

An engineered transforming growth factor β (TGF-β) monomer that functions as a dominant negative to block TGF-β signaling.
Kim et al. (2017)
2 more