› 6p6c

Solution NMR

CS-Rosetta Model of PEA-15 Death Effector Domain in the Complex with ERK2

Released:
DOI: 10.2210/pdb6p6c/pdb
PDB entry 6p6c coloured by chain, ensemble of 10 models, front view.
PDB entry 6p6c coloured by chain, ensemble of 10 models, side view.
PDB entry 6p6c coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
PEA-15 C-Terminal Tail Allosterically Modulates Death-Effector Domain Conformation and Facilitates Protein-Protein Interactions.
Crespo-Flores SL, Cabezas A, Hassan S, Wei Y
Int J Mol Sci 20 (2019)
PMID: 31284641

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172223 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Astrocytic phosphoprotein PEA-15 Chain: A
Molecule details ›
Chain: A
Length: 130 amino acids
Theoretical weight: 15.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q15121 (Residues: 1-130; Coverage: 100%)
Gene name: PEA15
Sequence domains: Death effector domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 26%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

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Citations

1 citations in other articles

Phosphorylation of PED/PEA-15 at Ser116 and phosphorylation of p27 at Thr187 indicates a poor prognosis in hepatocellular carcinoma.
Wu et al. (2021)

2 mentions without citation

PEA-15 C-Terminal Tail Allosterically Modulates Death-Effector Domain Conformation and Facilitates Protein-Protein Interactions.
Crespo-Flores et al. (2019)
1 more