Histone methyltransferase: Difference between revisions

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<StructureSection load='1o9s' size='350' side='right' caption='Human histone-lysine N-methyltrasferase (magenta) complex with methylated lysine histone H3 peptide (green) and S-adenosyl homocysteine (SAH) (PDB entry [[1o9s]])' scene='46/467278/Cv/1'>
<StructureSection load='' size='350' side='right' caption='Human histone-lysine N-methyltrasferase (magenta) complex with methylated lysine histone H3 peptide (green) and S-adenosyl homocysteine (SAH) (PDB entry [[1o9s]])' scene='46/467278/Cv/1'>


== Function ==
== Function ==
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**[[4gnd]] - hKHMT Nsd3 Phd5-C5HCH<br />
**[[4gnd]] - hKHMT Nsd3 Phd5-C5HCH<br />
**[[4rxj]] - hKHMT Nsd3 residues 953-1064<br />
**[[4rxj]] - hKHMT Nsd3 residues 953-1064<br />
**[[4yz8]], [[5upd]] - hKHMT Nsd3 residues 1054-1285<br />
**[[5upd]]- hKHMT Nsd3 residues 1054-1285<br />
**[[3lqh]] - hKHMT Mll Phd bromodomain<br />
**[[3lqh]] - hKHMT Mll Phd bromodomain<br />
**[[3b7b]] - hKHMT ankyrin repeat domains 2-7<br />
**[[3b7b]] - hKHMT ankyrin repeat domains 2-7<br />

Revision as of 22:00, 28 December 2017


Function

Histone methyltransferase (HMT) are histone-lysine N-methyltransferase (KHMT) and histone-arginine N-methyltransferase (RHMT) which catalyzes the transfer of methyl groups to lysine and arginine residues of histones[1]. HMT use S-adenosyl methionine (SAM) or S-adenosyl homocysteine (SAH) as the methyl donor. KHMT can be SET domain-containing or non-SET domain-containing. The SET domain contains the catalytic core of KHMT and targets the lysine tail region of KHMT. CxxC domain is a zinc finger domain.

Relevance

Inhibitors of the histone-lysine N-methyltransferase SMYD2 which represses the tumor-suppressing activities of p53 are studied as cancer therapy drugs[2].

Disease

Aberrant HMT plays a role in cancer, intellectual disability syndromes and regulation of tissue aging[3].

Structural highlights

Human inserted in a hydrophobic environment[4]. Water molecules shown as red spheres

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

Drag the structure with the mouse to rotate

3D Structures of histone methyltransferase3D Structures of histone methyltransferase

Updated on 28-December-2017

ReferencesReferences

  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

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Michal Harel, Alexander Berchansky, Joel L. Sussman
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