k d = 23 µm
DESCRIPTION
ITC characterization of L3MBTL2 4MBT binding with different histone peptides. H3K4me1. H3K9me1. H3K27me1. H3K9me2. H3K27me2. K D = 23 µM. K D = 43 µM. K D = 56 µM. K D = 9 µM. K D = 38 µM. Supplementary Figure 3a. Monomethylated Lysine interaction with L3MBTL2. - PowerPoint PPT PresentationTRANSCRIPT
0 1 2 3 4 5 6 7 8
-4
-2
0
-1.5
-1.2
-0.9
-0.6
-0.3
0.0
-10 0 10 20 30 40 50 60 70 80
Time (min)
µcal/sec
Molar Ratio
kcal/mole of injectantKD = 23 µM
H3K4me1
0 5 10 15 20 25-2
-1
0
-1.8
-1.5
-1.2
-0.9
-0.6
-0.3
0.0
-10 0 10 20 30 40 50 60 70 80
Time (min)
Molar Ratio
H3K9me1
KD = 43 µM
0 1 2 3 4 5 6 7
-4
-2
0
-1.2
-0.9
-0.6
-0.3
0.0
-10 0 10 20 30 40 50 60 70 80
Time (min)
Molar Ratio
KD = 9 µM
H3K9me2
0 1 2 3 4 5-1.0
-0.8
-0.6
-0.4
-0.2
0.0
0.2-0.8
-0.6
-0.4
-0.2
0.0
-10 0 10 20 30 40 50 60 70 80
Time (min)
Molar Ratio
KD = 56 µM
0 1 2 3 4 5
-1.2
-1.0
-0.8
-0.6
-0.4
-0.2
0.0
0.2-1.0
-0.8
-0.6
-0.4
-0.2
0.0
-10 0 10 20 30 40 50 60 70 80
Time (min)
Molar Ratio
KD = 38 µM
H3K27me1 H3K27me2
Supplementary Figure 3a
ITC characterization of L3MBTL2 4MBT binding with different histone peptides
The binding of monomethylated lysine to L3MBTl2 is very weak (~4000 uM)
Monomethylated Lysine interaction with L3MBTL2
Supplementary Figure 3b
0 2 4 6 8 10-0.30
-0.24
-0.18
-0.12
-0.06
-1.0
-0.8
-0.6
-0.4
-0.2
0.0
0 10 20 30 40 50 60 70 80
Time (min)
µcal/sec
Molar Ratio
kcal/mole of injectant
KD (µM) N ∆H
(cal . mol-1)
∆S
(cal . mol-1)
∆G
(cal . mol-1 . K-1)
H3K4me
H3K9me
H4K20me
H4K27me
H3K9me2
H4K20me2
H4K27me2
23
43
14
56
9
11
38
1.1
1.1
0.9
1.2
1.0
1.2
0.9
-6921
-5047
-15000
-1309
-5083
-3585
-1805
-2
3
-33
15
6
11
14
-6330
-5940
-5170
-5780
-6870
-6710
-5980
Thermodynamic parameters of the interaction of L3MBTL2 with histone peptides
Supplementary Figure 3c