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. Author manuscript; available in PMC: 2015 Jan 7.

Published in final edited form as: Structure. 2013 Nov 7;22(1):82–93. doi: 10.1016/j.str.2013.09.019

Table 1.

FP binding affinities of CALP and NHERF PDZ domains for iCAL36/CFTR chimeric peptides.

		K_i (μM)
Peptide^a	Sequence^b	CALP	CALP E317A	N1P1	N1P2	N2P1	N2P2
iCAL36_TRL	ANSRWPTTRL	4.5 ± 0.8	2.2 ± 1.2	8.0 ± 1.4	110 ± 10	8.7 ± 3.1	16.5 ± 3.9
iCAL36_Q^-4	ANSRWQTSII	14.8 ± 3.5	ND^d	280 ± 100	>1000	300 ± 100	450 ± 150
CFTR_T^-3	TEEEVQTTRL	18 ± 5.5	15.1 ± 2.0	0.76 ± 0.51	4.6 ± 1.6	1.3 ± 0.4	0.45 ± 0.25
iCAL36^c	ANSRWPTSII	22.6 ± 8.0	15.1 ± 2.1	>1000	>1000	>1000	>1000
iCAL36_L^c	ANSRWPTSIL	23.6 ± 2.2	ND^d	230 ± 100	>1000	76.8 ± 1.6	530 ± 120
iCAL36_QDTRL	ANSRWQDTRL	56.2 ± 5.6	16.2 ± 3.5	1.5 ± 0.2	6.7 ± 2.4	3.1 ± 1.4	1.1 ± 0.6
iCAL36_VQDTRL	ANSRVQDTRL	230 ± 30	140 ± 40	2.5 ± 0.3	6.5 ± 2.3	3.8 ± 1.4	0.94 ± 0.42
CFTR^c	TEEEVQDTRL	420 ± 80	64.7 ± 1.8	0.47 ± 0.2	1.8 ± 0.5	0.83 ± 0.33	0.07 ± 0.05
CFTR_I^c	TEEEVQDTRI	490 ± 120	ND^d	10.7 ± 2.8	39.8 ± 1.0	19.1 ± 2.9	2.5 ± 0.43
iCAL36_VQD^-3	ANSRVQDSII	>1000	770 ± 50	>1000	>1000	>1000	420 ± 120

^a

Substitutions noted in subscript; the final substituted position is C-terminal unless numbered.

^b

Bold indicates residue(s) from the CFTR sequence; non-bold indicates residues from iCAL36.

^c

Values previously reported in Amacher et al., 2013.

^d

ND indicates that value was not measured.