Fig. 7: The ssK36 peptide-SETD2 complex establishes significantly more SN2 TS-like structures than the H3K36 peptide. | Communications Chemistry

Fig. 7: The ssK36 peptide-SETD2 complex establishes significantly more SN2 TS-like structures than the H3K36 peptide.

From: Mechanistic basis of the increased methylation activity of the SETD2 protein lysine methyltransferase towards a designed super-substrate peptide

Fig. 7

a Model of SETD2 complexed with ssK36 derived from crystal structure PDB: 6VDB. b Model of SETD2 complexed with H3K36 derived from crystal structure PDB: 5V21. c Number of TS-like structures reached in MD simulations of the ssK36 and H3K36-SETD2 complexes. The graph shows the average of 15 simulations à 100 ns. Error bars represent the SEM (p-value 1.2 × 10−8, based on two-tailed t-Test with equal variance). d Stability of TS-like conformations formed by SETD2-H3K36 and SETD2-ssK36 complexes as determined by the distribution of events with TS-like conformations persisting over a given number of consecutive MD frames. Note the strong overrepresentation of long-living TS-like conformations of ssK36 (highlighted by the red box).

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