Table 1 ITC derived apparent dissociation constants for each step of the TAPBPR-mediated peptide exchange cycle.

From: TAPBPR promotes antigen loading on MHC-I molecules using a peptide trap

 

TAPBPRWT

n value

TAPBPRΔG24-R36

n value

TAX8 KD1,app

37.4 nM

n/d

13.9 nM

n/d

TAX9 KD1,app

30.6 nM

n/d

11.1 nM

n/d

KLL15 KD1,app

38.8 nM

n/d

14.2 nM

n/d

TAX8 KD2,app

326 ± 14 nM

0.43 ± 0.02

316 ± 19 nM

0.44 ± 0.03

TAX9 KD2,app

40.2 ± 6.5 nM

0.42 ± 0.01

42.6 ± 8.3 nM

0.46 ± 0.01

KLL15 KD2,app

383 ± 22 nM

0.45 ± 0.06

334 ± 20 nM

0.41 ± 0.01

TAX8 KD3

2.6 ± 0.5 µM

1.00 ± 0.03

2.4 ± 0.6 µM

1.03 ± 0.01

TAX9 KD3

1.9 ± 0.7 µM

1.02 ± 0.01

1.8 ± 0.3 µM

1.06 ± 0.02

KLL15 KD3

2.2 ± 0.5 µM

1.05 ± 0.04

2.1 ± 0.3 µM

1.03 ± 0.01

TAX8 KD4

22.7 ± 8.2 µM

1.01 ± 0.02

54.4 ± 9.4 µM

1.05 ± 0.02

TAX9 KD4

2.5 ± 0.8 µM

1.04 ± 0.01

7.3 ± 0.7 µM

1.02 ± 0.02

KLL15 KD4

21.6 ± 7.0 µM

1.10 ± 0.05

49.5 ± 8.6 µM

1.03 ± 0.04

  1. TAX8 = LFGYPVYV
  2. TAX9 = LLFGYPVYV
  3. KLL15 = KLLEIPDPDKNWATL
  4. WT = wild-type
  5. Due to experimental limitations, the measured KD1 and KD2 values are “apparent”, denoted with the use of “app”.
  6. n/d not determined because the KD1 value is calculated from thermodynamic balance, n value corresponds to observed stoichiometry by ITC.