Fig. 9: Summary of the results of this study. | Communications Chemistry

Fig. 9: Summary of the results of this study.

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

Fig. 9

a Preferred hairpin formation of ssK36 in solution due to favourable intrapeptide contacts. b Accelerated binding of the hairpin into the SETD2 peptide binding cleft with the K36 facing outside. c Unfolding of the hairpin conformation in the SETD2-peptide complex by specific enzyme-peptide contacts in a zipper-like process leading to the adoption of an extended peptide conformation. d Distinct contact networks lead to different TS-like conformations and better stabilization of TS-like conformation of ssK36 than H3K36.

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