This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1muf
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1muf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1muf, resolution 2.26Å" /> '''Structure of histon...)
Next diff →
Revision as of 16:08, 12 November 2007
|
Structure of histone H3 K4-specific methyltransferase SET7/9
Overview
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.
About this Structure
1MUF is a Single protein structure of sequence from Homo sapiens. Active as Histone-lysine N-methyltransferase, with EC number 2.1.1.43 Full crystallographic information is available from OCA.
Reference
The active site of the SET domain is constructed on a knot., Jacobs SA, Harp JM, Devarakonda S, Kim Y, Rastinejad F, Khorasanizadeh S, Nat Struct Biol. 2002 Nov;9(11):833-8. PMID:12389038
Page seeded by OCA on Mon Nov 12 18:15:04 2007
