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Literature summary for 7.6.2.2 extracted from
- P-glycoprotein retains drug-stimulated ATPase activity upon covalent linkage of the two nucleotide binding domains at their C-terminal ends (2011), J. Biol. Chem., 286, 10476-10482.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | introduction of cysteine residues into Cys-less P-glycoprotein and cysteine-mediated cross-linking. For mutant A627C/S1276C, disulfide formation is with high efficiency and cross-linked P-glycoprotein retains 30-68% drug-stimulated ATPase activity compared with reduced or cysteine-less P-glycoprotein. Cysteine pairs K615C/S1276C and A627C/K1260C also form a disulfide, but to a lesser extent, and the cross-linked form of these two mutants have lower drug-stimulated ATPase activity | Mus musculus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Mdr3 | - |
Mus musculus |
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Release 2023.1 (January 2023)
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