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Fig. 2 | Biology Direct

Fig. 2

From: Intrinsic protein disorder in histone lysine methylation

Fig. 2

Molecular dynamics simulation of MLL1-menin-LEDGF/p75 complex. a Overlay of 20 structures between 900 k-1100 k steps of DMD of free MLL1 N-terminus. The region between amino acids 120–135 are highlighted in red or orange. b DSSP helix content of the free MLL1 N-terminus per frame versus the amino acid chain. Orange to red lines represent the number of replicas (one, two or three) in any given frame that contain an amino acid in helical conformation (1–2000 k steps). c Structure of the ternary complex as represented in PDB database (3U88). Salmon: MLL1, cyan: LEDGF/p75, green: menin. Side chains of F148 and F151 in MLL1 are red. Intramolecular contacts are shown as yellow-red dots. d Structure of the ternary complex as modeled with the disordered regions of MLL1 based on PDB structures 3U88 and 2MSR. Salmon: MLL1, cyan: LEDGF/p75, green: menin. Side chains of F148 and F151 in MLL1 are red. Intramolecular contacts are shown as yellow-red dots (at 200 k steps)

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