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Histone methyltransferase

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(New page: '''Histone methyltransferase''' (HMT) are histone-lysine N-methyltransferase (KHMT) and histone-arginine N-methyltransferase (RHMT) which catalyzes the transfer of methyl groups to ly...)
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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]] }}
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'''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.
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'''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.
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== 3D Structures of histone methyltransferase ==
[[1nw3]] – hHMT DOT1L – human
[[1nw3]] – hHMT DOT1L – human
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[[3s7j]], [[3tg4]] - hKHMT Smyd2 + SAM
[[3s7j]], [[3tg4]] - hKHMT Smyd2 + SAM
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[[Category:Topic Page]]

Revision as of 21:37, 29 September 2011

Template:STRUCTURE 3s7j

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.

Contents

3D Structures of histone methyltransferase

1nw3 – hHMT DOT1L – human

2igq – hHMT-1 C terminal

Histone-lysine N-methyltransferase

2j8a – KHMT SET1 RRM domain – yeast

3s8s – hKHMT SETD1A RRM domain

3rib – hKHMT Smyd2 + SAH

3s7b - hKHMT Smyd2 + SAM + inhibitor

3s7d, 3s7f, 3tg5 - hKHMT Smyd2 + SAH + p53 peptide

3s7j, 3tg4 - hKHMT Smyd2 + SAM

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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