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Literature summary for 7.6.2.2 extracted from
- The ATPase activity of the P-glycoprotein drug pump is highly activated when the N-terminal and central regions of the nucleotide-binding domains are linked closely together (2012), J. Biol. Chem., 287, 26806-26816.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in HEK-293 cell | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C137A/C431A/C717A/C956A/C1074A/C1125A/C1227A | replacement of the seven endogenous cysteines to create a Cys-less P-gp. Intoduction of new cysteine residues in different domains and disulfide cross-linking with short or long cross-linkers shows that cross-linking of cysteines that lie close to the LSGGQ signature sequne, such as P517C, and Walker A, such as I1050C, sites of NBD1 and NBD2 respectively, as well as thecytoplasmic extensions of TM segments 3, D177C or L175C, and 9, N820C, with a shortcross-linker activat ATPase activity over 10fold. Cross-linking between the NBDs is not inhibited by tariquidar. Cross-linking between extracellular cysteines, mutant T333C/L975C, predicted to lock P-gp into a conformation that prevents close NBD association inhibit ATPase activity | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
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Release 2023.1 (January 2023)
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