› 1e9k

Solution NMR

The structure of the RACK1 interaction sites located within the unique N-terminal region of the cAMP-specific phosphodiesterase, PDE4D5.

Released:
DOI: 10.2210/pdb1e9k/pdb
PDB entry 1e9k coloured by chain, front view.
PDB entry 1e9k coloured by chain, side view.
PDB entry 1e9k coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
1H NMR structural and functional characterisation of a cAMP-specific phosphodiesterase-4D5 (PDE4D5) N-terminal region peptide that disrupts PDE4D5 interaction with the signalling scaffold proteins, beta-arrestin and RACK1.
Smith KJ, Baillie GS, Hyde EI, Li X, Houslay TM, McCahill A, Dunlop AJ, Bolger GB, Klussmann E, Adams DR, Houslay MD
Cell Signal 19 2612-24 (2007)
PMID: 17900862

Function and Biology Details

Reaction catalysed: 
Adenosine 3',5'-cyclic phosphate + H(2)O = adenosine 5'-phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170654 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3',5'-cyclic-AMP phosphodiesterase 4D Chain: A
Molecule details ›
Chain: A
Length: 38 amino acids
Theoretical weight: 4.43 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q08499 (Residues: 250-265, 266-280; Coverage: 4%)
Gene names: DPDE3, PDE4D

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Not provided

Quick links

Citations

8 review citations

Underpinning compartmentalised cAMP signalling through targeted cAMP breakdown.
Houslay MD. (2010)
7 more

1 mention without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)