TY - JOUR
AU - Khorasanizadeh, Sepideh
AB - The SET domain contains the catalytic center of lysine methyltransferases that target the N-terminal tails of histones and regulate chromatin function. Here we report the structure of the SET7/9 protein in the absence and presence of its cofactor product, S-adenosyl-L-homocysteine (AdoHcy). A knot within the SET domain helps form the methyltransferase active site, where AdoHcy binds and lysine methylation is likely to occur. A structure-guided comparison of sequences within the SET protein family suggests that the knot substructure and active site environment are conserved features of the SET domain.
TI - The active site of the SET domain is constructed on a knot
JF - Nature Structural & Molecular Biology
DO - 10.1038/nsb861
DA - 2002-10-21
UR - https://www.deepdyve.com/lp/springer-journals/the-active-site-of-the-set-domain-is-constructed-on-a-knot-buR6DkI9rf
SP - 833
EP - 838
VL - 9
IS - 11
DP - DeepDyve
ER -