Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | the active sites of PTPs are exceptionally conserved and charged, making it nearly impossible to develop PTP inhibitors that are selective. But targeting PTP protein (substrate/regulatory) interaction sites, which are distal from the active sites, are highly viable and suitable drug targets. Domains outside PTP catalytic domains have also been demonstrated to directly alter PTP activity. Development of drugs that bind to intrinsically disordered regions of the enzyme, overview | Homo sapiens | |
MSI-1436 | small molecule inhibitor MSI-1436 binds to the disordered C-terminal domain of PTP1B, C-terminal to the catalytic domain, MSI-1436 functions using an allosteric mechanism to direct the enzymatic activity of PTP1B | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
[a protein]-tyrosine phosphate + H2O | Homo sapiens | - |
[a protein]-tyrosine + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P18031 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
[a protein]-tyrosine phosphate + H2O | - |
Homo sapiens | [a protein]-tyrosine + phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
protein tyrosine phosphatase | - |
Homo sapiens |
PTP1B | - |
Homo sapiens |