3OPE

Structural Basis of Auto-inhibitory mechanism of Histone methyltransferase

3OPE の概要

• エントリーDOI: 10.2210/pdb3ope/pdb
• 分子名称: Probable histone-lysine N-methyltransferase ASH1L, ZINC ION, S-ADENOSYLMETHIONINE, ... (4 entities in total)
• 機能のキーワード: set, methyltransferase, nucleus, transferase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 52561.55

構造登録者

An, S.,Song, J. (登録日: 2010-08-31, 公開日: 2011-01-12, 最終更新日: 2024-03-20)

主引用文献

An, S.,Yeo, K.J.,Jeon, Y.H.,Song, J.
Crystal structure of the human histone methyltransferase ASH1L catalytic domain and its implications for the regulatory mechanism
J.Biol.Chem., 286:8369-8374, 2011

PubMed Abstract: Absent, small, or homeotic disc1 (Ash1) is a trithorax group histone methyltransferase that is involved in gene activation. Although there are many known histone methyltransferases, their regulatory mechanisms are poorly understood. Here, we present the crystal structure of the human ASH1L catalytic domain, showing its substrate binding pocket blocked by a loop from the post-SET domain. In this configuration, the loop limits substrate access to the active site. Mutagenesis of the loop stimulates ASH1L histone methyltransferase activity, suggesting that ASH1L activity may be regulated through the loop from the post-SET domain. In addition, we show that human ASH1L specifically methylates histone H3 Lys-36. Our data implicate that there may be a regulatory mechanism of ASH1L histone methyltransferases.

PubMed: 21239497
DOI: 10.1074/jbc.M110.203380

実験手法

X-RAY DIFFRACTION (2.9 Å)