Table 1.
Description for the four mutants used during the study.
| System Name | Description Per Subunit |
Mutant Type | Tyrosine in Both Subunit |
|---|---|---|---|
| 2loop2 | 1 Y in 1st PD1 1 Y in 2nd PD2 |
- | 4 (2 per monomer) |
| 2loop2/Y99A | 1 A in 1st PD1 1 Y in 2nd PD2 |
Y99A | 2 (1 per monomer) |
| 2loop2/Y205A | 1 Y in 1st PD1 1 A in 2nd PD2 |
- Y205A |
2 (1 per monomer) |
| 2loop2/Y99A/Y205A | 1 A in 1st PD1 1 A in 2nd PD2 |
Y99A Y205A |
0 (0 per monomer) |
In construct named 2loop2, the cap structure from TASK-3 channels was removed and the 1st Pore Domain (PD1) was replaced by 2nd Pore Domain (PD2). Hence, 2loop2 has two PD2 with 2 Tyr (Tyrosine) residues (Y99 & Y205) per subunit, forming the putative binding site of TEA. In the mutant 2loop2/Y99A, the Y99 was mutated to alanine in both subunits (Y99AA, Y99AB). In 2loop2/Y205A, the Y205 was mutated to alanine and 2loop2/Y99A/Y205A, theY99 and Y205 were mutated by alanine in both subunits, generating a channel without a binding site for TEA.