Application | Comment | Organism |
---|---|---|
medicine | interactions of PDE4D5 with both the N- and C-terminal domains of beta-arrestin are essential for beta2-adrenoceptor regulation | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli as N-terminal glutathione S-transferase-fusion protein | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Homo sapiens | interaction of PDE4D5 with both the N- and C-domains of beta-arrestin 2 are essential for beta2-adrenoceptor regulation | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
isoforms PDE4D3 and PDE4D5 | - |
Homo sapiens | Q08499 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | interaction of PDE4D5 with both the N- and C-domains of beta-arrestin 2 are essential for beta2-adrenoceptor regulation | Homo sapiens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | isoform PDE4D interacts with beta-arrestin. Identification of a binding site in the beta-arrestin 2 N-domain for the common PDE4D catalytic unit and two regions in the beta-arrestin 2 C domain that confer specificity for PDE4D5 binding. Reduced interaction of PDE4D5 with beta-arrestin mutants R26A, K18A, or T20A. R286, D291, and L215-H220 of beta-arrestin are important for binding PDE4D5, but not for PDE4D3. Interactions of PDE4D5 with both the N- and C-terminal domains of beta-arrestin are essential for beta2-adrenoceptor regulation | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
PDE4D5 | - |
Homo sapiens |