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. Author manuscript; available in PMC: 2013 Jan 11.
Published in final edited form as: Structure. 2012 Jan 11;20(1):41–55. doi: 10.1016/j.str.2011.11.013

Table 3.

Thermodynamic parameters of wild-type and mutant EphA2:SHIP2 SAM:SAM complex measured by ITC.

Eph SAM domain SHIP2 Kd (μM) ΔH (kcal/mol) TΔS (kcal/mol) ΔG (kcal/mol)
I. Characterizing SAM:SAM interaction
EphA2 WT WT 5.2 ± 1.2 −2.5 4.7 −7.2
EphA2 WT D1223A/D1224A Non-binding - - -
EphA1 WT 3.8 ± 0.4 −3.6 3.8 −7.4
II. Interactions between ion pairs EphA2:SHIP2 mutants
P952A/K956E WT Non-binding - - -
K917E/P952A/K956E WT Non-binding - - -
R950E WT 1.7 ± 0.3 −2.4 5.5 −7.9
R950E H1219R 1.3 ± 0.1 −5.0 3.0 −8.0
R950E H1219E 11.2 ± 2.7 −7.5 −0.8 −6.7
WT H1219E 4.0 ± 0.4 −5.5 1.8 −7.3
III. Interaction manipulation
EphB2 WT Non-binding - - -
EphB2 mutanta WT 7.6 ± 2.5 −0.9 6.1 −7.0
EphA2 Y960N WT 3.1 ± 0.4 −3.0 4.5 −7.5
EphA2 K945L WT 1.3 ± 0.2 −2.1 5.9 −8.0
EphA2 K945L/Y960N WT 1.6 ± 0.6 −2.0 5.9 −7.9
a

: EphB2 penta-mutant, L954K/T959R/A961P/K966R/N969Y. The mutated residues correspond to EphA2 K945, R950, P952, R957 and Y960.