2ODD

Solution structure of the MYND domain from AML1-ETO complexed with SMRT, a corepressor

2ODD の概要

• エントリーDOI: 10.2210/pdb2odd/pdb
• 関連するPDBエントリー: 2OD1
• 分子名称: SMRT, Protein CBFA2T1, ZINC ION (3 entities in total)
• 機能のキーワード: mynd zinc finger, cross-braced topology, poly-proline, proline-tryptophan interaction, metal binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus (Potential): Q06455
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 9105.61

構造登録者

Liu, Y.Z.,Chen, W.,Gaudet, J.,Cheney, M.D.,Roudaia, L.,Cierpicki, T.,Klet, R.C.,Hartman, K.,Laue, T.M.,Speck, N.A.,Bushweller, J.H. (登録日: 2006-12-22, 公開日: 2007-06-19, 最終更新日: 2023-12-27)

主引用文献

Liu, Y.,Chen, W.,Gaudet, J.,Cheney, M.D.,Roudaia, L.,Cierpicki, T.,Klet, R.C.,Hartman, K.,Laue, T.M.,Speck, N.A.,Bushweller, J.H.
Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity.
Cancer Cell, 11:483-497, 2007

PubMed Abstract: AML1/ETO results from the t(8;21) associated with 12%-15% of acute myeloid leukemia. The AML1/ETO MYND domain mediates interactions with the corepressors SMRT and N-CoR and contributes to AML1/ETO's ability to repress proliferation and differentiation of primary bone marrow cells as well as to enhance their self renewal in vitro. We solved the solution structure of the MYND domain and show it to be structurally homologous to the PHD and RING finger families of proteins. We also determined the solution structure of an MYND-SMRT peptide complex. We demonstrated that a single amino acid substitution that disrupts the interaction between the MYND domain and the SMRT peptide attenuated AML1/ETO's effects on proliferation, differentiation, and gene expression.

PubMed: 17560331
DOI: 10.1016/j.ccr.2007.04.010

実験手法

SOLUTION NMR