› 7ta3

X-ray diffraction
2.5Å resolution

Trimer-to-Monomer Disruption of Tumor Necrosis Factor-alpha (TNF-alpha) by alpha-peptide-3

Released:
DOI: 10.2210/pdb7ta3/pdb
PDB entry 7ta3 coloured by chain, front view.
PDB entry 7ta3 coloured by chain, side view.
PDB entry 7ta3 coloured by chain, top view.
Source organisms:
Primary publication:
Trimer-to-Monomer Disruption Mechanism for a Potent, Protease-Resistant Antagonist of Tumor Necrosis Factor-α Signaling.
Niu J, Cederstrand AJ, Eddinger GA, Yin B, Checco JW, Bingman CA, Outlaw VK, Gellman SH
J Am Chem Soc 144 9610-9617 (2022)
PMID: 35613436

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134277 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Alpha-peptide-3 Chains: A, C
Molecule details ›
Chains: A, C
Length: 32 amino acids
Theoretical weight: 3.6 KDa
Source organism: synthetic construct
Expression system: Not provided
Tumor necrosis factor, soluble form Chains: B, D
Molecule details ›
Chains: B, D
Length: 158 amino acids
Theoretical weight: 17.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01375 (Residues: 77-233; Coverage: 67%)
Gene names: TNF, TNFA, TNFSF2
Sequence domains: TNF(Tumour Necrosis Factor) family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P43212
Unit cell:
a: 86.56Å b: 86.56Å c: 143.73Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.249 0.246 0.277
Expression systems:
  • Not provided
  • Escherichia coli

Quick links

Citations

1 citations in other articles

Sulfono-γ-AApeptides as Protein Helical Domain Mimetics to Manipulate the Angiogenesis.
Xue et al. (2022)

1 mention without citation

Trimer-to-Monomer Disruption Mechanism for a Potent, Protease-Resistant Antagonist of Tumor Necrosis Factor-α Signaling.
Niu et al. (2022)