期刊
CANCER CELL
卷 11, 期 6, 页码 483-497出版社
CELL PRESS
DOI: 10.1016/j.ccr.2007.04.010
关键词
-
资金
- NCI NIH HHS [R01 CA108056-01, R01 CA108056-02, R01 CA108056, R01 CA108056-04, R01 CA108056-03] Funding Source: Medline
- NIAMS NIH HHS [T32 AR007576, T32 AR07576] Funding Source: Medline
- NIGMS NIH HHS [T32 GM008704, T32 GM08704] Funding Source: Medline
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据