Histone methyltransferase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 5: Line 5:
== Relevance ==
== Relevance ==
-
Inhibitors of the histone-lysine N-methyltransferase SMYD2 which represses the tumor-suppressing activities of p53 are studied as cancer therapy drug<ref>PMID:21782458</ref>.s.
+
Inhibitors of the histone-lysine N-methyltransferase SMYD2 which represses the tumor-suppressing activities of p53 are studied as cancer therapy drugs<ref>PMID:21782458</ref>.
== Disease ==
== Disease ==
Line 64: Line 64:
*Histone-lysine N-methyltransferase binary complexes
*Histone-lysine N-methyltransferase binary complexes
-
**[[2kkf]] – hKHMT Hrx CxxC domain +_DNA – NMR<br />
+
**[[2kkf]] – hKHMT Hrx CxxC domain + DNA – NMR<br />
**[[4nw3]] – hKHMT Mll CxxC domain + DNA <br />
**[[4nw3]] – hKHMT Mll CxxC domain + DNA <br />
**[[4pzi]] – hKHMT CxxC domain + DNA <br />
**[[4pzi]] – hKHMT CxxC domain + DNA <br />
-
**[[3q0b]], [[3q0c]], [[3q0d]], [[3q0f]] – hKHMT SRA domain +_DNA <br />
+
**[[3q0b]], [[3q0c]], [[3q0d]], [[3q0f]] – hKHMT SRA domain + DNA <br />
**[[3qow]] – hKHMT + SAM <br />
**[[3qow]] – hKHMT + SAM <br />
**[[4fmu]] – hKHMT SETD2 + inhibitor <br />
**[[4fmu]] – hKHMT SETD2 + inhibitor <br />

Revision as of 09:40, 24 March 2016

Human histone-lysine N-methyltrasferase (grey, green) complex with methylated lysine histone H3 peptide (rust, aqua) and S-adenosyl homocysteine (SAH) (PDB entry 1o9s)

Drag the structure with the mouse to rotate

3D Structures of histone methyltransferase

Updated on 24-March-2016

References

  1. Trievel RC. Structure and function of histone methyltransferases. Crit Rev Eukaryot Gene Expr. 2004;14(3):147-69. PMID:15248813
  2. Ferguson AD, Larsen NA, Howard T, Pollard H, Green I, Grande C, Cheung T, Garcia-Arenas R, Cowen S, Wu J, Godin R, Chen H, Keen N. Structural Basis of Substrate Methylation and Inhibition of SMYD2. Structure. 2011 Jul 20. PMID:21782458 doi:10.1016/j.str.2011.06.011
  3. Greer EL, Shi Y. Histone methylation: a dynamic mark in health, disease and inheritance. Nat Rev Genet. 2012 Apr 3;13(5):343-57. doi: 10.1038/nrg3173. PMID:22473383 doi:http://dx.doi.org/10.1038/nrg3173
  4. Xiao B, Jing C, Wilson JR, Walker PA, Vasisht N, Kelly G, Howell S, Taylor IA, Blackburn GM, Gamblin SJ. Structure and catalytic mechanism of the human histone methyltransferase SET7/9. Nature. 2003 Feb 6;421(6923):652-6. Epub 2003 Jan 22. PMID:12540855 doi:10.1038/nature01378

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

Personal tools