› 1f2h

Solution NMR

SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE TNFR1 ASSOCIATED PROTEIN, TRADD.

Released:
DOI: 10.2210/pdb1f2h/pdb
PDB entry 1f2h coloured by chain, front view.
PDB entry 1f2h coloured by chain, side view.
PDB entry 1f2h coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of N-TRADD and characterization of the interaction of N-TRADD and C-TRAF2, a key step in the TNFR1 signaling pathway.
Tsao DH, McDonagh T, Telliez JB, Hsu S, Malakian K, Xu GY, Lin LL
Mol Cell 5 1051-7 (2000)
PMID: 10911999

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172342 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tumor necrosis factor receptor type 1-associated DEATH domain protein Chain: A
Molecule details ›
Chain: A
Length: 169 amino acids
Theoretical weight: 18.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q15628 (Residues: 1-169; Coverage: 54%)
Gene name: TRADD
Sequence domains: TRADD, N-terminal domain
Structure domains: TRADD, N-terminal domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

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

Quick links

Citations

11 review citations

The TNF-receptor-associated factor family: scaffold molecules for cytokine receptors, kinases and their regulators.
Wajant et al. (2001)
10 more

3 mentions without citation

Functional roles in cell signaling of adaptor protein TRADD from a structural perspective.
Li et al. (2020)
2 more