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Histone methyltransferase
From Proteopedia
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{{STRUCTURE_3s7j| PDB=3s7j | SIZE=400| SCENE= |right|CAPTION=Human histone-lysine N-methyltrasferase Smyd2 complex with S-adenosyl methionine, [[3s7j]] }} | {{STRUCTURE_3s7j| PDB=3s7j | SIZE=400| SCENE= |right|CAPTION=Human histone-lysine N-methyltrasferase Smyd2 complex with S-adenosyl methionine, [[3s7j]] }} | ||
| - | + | == 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. 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. | + | '''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<ref>PMID:15248813</ref>. 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. |
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| - | + | == References == | |
| + | <references/> | ||
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Revision as of 08:50, 24 March 2016
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.
3D Structures of histone methyltransferase
Updated on 24-March-2016
References
- ↑ Trievel RC. Structure and function of histone methyltransferases. Crit Rev Eukaryot Gene Expr. 2004;14(3):147-69. PMID:15248813
