› 7ta6

X-ray diffraction
2.67Å resolution

Trimer-to-Monomer Disruption of Tumor Necrosis Factor-alpha (TNF-alpha) by unnatural alpha/beta-peptide-1

Released:
DOI: 10.2210/pdb7ta6/pdb
PDB entry 7ta6 coloured by chain, front view.
PDB entry 7ta6 coloured by chain, side view.
PDB entry 7ta6 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-524997 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tumor necrosis factor, soluble form Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
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
Alpha/Beta-peptide-1 Chains: I, J, K, L, M, N, O, P
Molecule details ›
Chains: I, J, K, L, M, N, O, P
Length: 29 amino acids
Theoretical weight: 3.29 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

3 bound ligands:
Ligand EDO 8 x EDO
Ligand K 1 x K
Ligand NH2 8 x NH2
1 modified residue:
Ligand AIB 24 x AIB

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: C2
Unit cell:
a: 143.774Å b: 143.552Å c: 76.888Å
α: 90° β: 97.85° γ: 90°
R-values:
R R work R free
0.246 0.245 0.273
Expression systems:
  • Escherichia coli
  • Not provided

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)