› 2l5s

Solution NMR

Solution structure of the extracellular domain of the TGF-beta type I receptor

Released:
DOI: 10.2210/pdb2l5s/pdb
PDB entry 2l5s coloured by chain, ensemble of 10 models, front view.
PDB entry 2l5s coloured by chain, ensemble of 10 models, side view.
PDB entry 2l5s coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
The TβR-I pre-helix extension is structurally ordered in the unbound form and its flanking prolines are essential for binding.
Zuniga JE, Ilangovan U, Mahlawat P, Hinck CS, Huang T, Groppe JC, McEwen DG, Hinck AP
J Mol Biol 412 601-18 (2011)
PMID: 21821041

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153250 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
TGF-beta receptor type-1 Chain: A
Molecule details ›
Chain: A
Length: 88 amino acids
Theoretical weight: 9.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P36897 (Residues: 31-115; Coverage: 17%)
Gene names: ALK5, SKR4, TGFBR1
Sequence domains: Activin types I and II receptor domain
Structure domains: CD59

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Promiscuity and specificity in BMP receptor activation.
Mueller et al. (2012)
3 more

3 mentions without citation

Structure-guided engineering of TGF-βs for the development of novel inhibitors and probing mechanism.
Hinck AP. (2018)
2 more