User:Mark Macbeth/Sandbox8: Difference between revisions
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===Active Site and Channel=== | ===Active Site and Channel=== | ||
[[Image:Methyl1.gif|300 px|left|Image of substrate bound on one side of SET7/9 with lysine target in the active site channel (Cyan) and S-adenosyl homocysteine (pink) bound on the other side of the enzyme]] | |||
The most notable feature of the HKMT is the presence of the lysine access channel as the active site. The cofactor and <scene name='81/811708/Sam_structure/3'>peptide</scene> substrate are actually located on opposite sides of the SET domain but are connected through this narrow channel (Figure 1).<ref name="Xiao" /> This channel allows these two components to interact and complete the methyltransfer. The active site in general is considerably tyrosine rich. Residues Tyr245, His297, Ser268, Tyr305, Tyr335, and Tyr337 all help to shape the <scene name='81/811707/Stick_active_site/2'>active site</scene> and the channel.<ref name="Xiao" /> The cofactor involved, SAM, provides the methyl for methylation of the lysine on its sulfur atom. | The most notable feature of the HKMT is the presence of the lysine access channel as the active site. The cofactor and <scene name='81/811708/Sam_structure/3'>peptide</scene> substrate are actually located on opposite sides of the SET domain but are connected through this narrow channel (Figure 1).<ref name="Xiao" /> This channel allows these two components to interact and complete the methyltransfer. The active site in general is considerably tyrosine rich. Residues Tyr245, His297, Ser268, Tyr305, Tyr335, and Tyr337 all help to shape the <scene name='81/811707/Stick_active_site/2'>active site</scene> and the channel.<ref name="Xiao" /> The cofactor involved, SAM, provides the methyl for methylation of the lysine on its sulfur atom. | ||
