Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.4.53 extracted from

  • Smith, K.J.; Baillie, G.S.; Hyde, E.I.; Li, X.; Houslay, T.M.; McCahill, A.; Dunlop, A.J.; Bolger, G.B.; Klussmann, E.; Adams, D.R.; Houslay, M.D.
    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 (2007), Cell. Signal., 19, 2612-2624.
    View publication on PubMed

Application

Application Comment Organism
molecular biology development of cell-permeable peptide reagents based upon the N-terminal region of PDE4D5 that allow for the selective disruption of PDE4D5 targeting to specific signalling scaffolds, namely beta-arrestin and RACK1 Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
NMR and CD analysis of the N-terminal 38mer peptide of isoform PDE4D5 which contains the entire signaling scaffold protein RACK1 interaction domain together with a portion of the beta-arrestin binding site. The peptiode has a distinct amphipathic helical structure. Study on binding to RACK1 and to beta-arrestin Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
isoform PDE4D5
-
Homo sapiens Q08499
-
-

Source Tissue

Source Tissue Comment Organism Textmining
HEK-293B2 cell
-
Homo sapiens
-

Synonyms

Synonyms Comment Organism
cAMP-specific phosphodiesterase-4D5
-
Homo sapiens
PDE4D5
-
Homo sapiens