› 4prz

X-ray diffraction
2.12Å resolution

Caspase-8 specific unnatural amino acid peptides

Released:
DOI: 10.2210/pdb4prz/pdb
PDB entry 4prz coloured by chain, front view.
PDB entry 4prz coloured by chain, side view.
PDB entry 4prz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Selective inhibition of initiator versus executioner caspases using small peptides containing unnatural amino acids.
Vickers CJ, González-Páez GE, Litwin KM, Umotoy JC, Coutsias EA, Wolan DW
ACS Chem Biol 9 2194-8 (2014)
PMID: 25079698

Function and Biology Details

Reaction catalysed: 
Strict requirement for Asp at position P1 and has a preferred cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-|-(Gly/Ser/Ala)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-165050 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Caspase-8 subunit p18 Chain: A
Molecule details ›
Chain: A
Length: 275 amino acids
Theoretical weight: 31.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14790 (Residues: 217-479; Coverage: 55%)
Gene names: CASP8, MCH5
Sequence domains: Caspase domain
Structure domains: Rossmann fold
(ACE)LET(1U8) PEPTIDE Chain: B
Molecule details ›
Chain: B
Length: 5 amino acids
Theoretical weight: 649 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand DTD 2 x DTD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P3121
Unit cell:
a: 62.145Å b: 62.145Å c: 129.383Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.191 0.19 0.218
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

5 review citations

Small Molecule Active Site Directed Tools for Studying Human Caspases.
Poreba et al. (2015)
4 more

4 mentions without citation

Carnosic Acid, a Natural Diterpene, Attenuates Arsenic-Induced Hepatotoxicity via Reducing Oxidative Stress, MAPK Activation, and Apoptotic Cell Death Pathway.
Das et al. (2018)
3 more