1WQ6

The tetramer structure of the nervy homolgy two (NHR2) domain of AML1-ETO is critical for AML1-ETO'S activity

Summary for 1WQ6

• Entry DOI: 10.2210/pdb1wq6/pdb
• Descriptor: AML1-ETO (2 entities in total)
• Functional Keywords: nhr2, eto, aml1-eto, oncoprotein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus (Potential): Q06455
• Total number of polymer chains: 2
• Total formula weight: 18307.46

Authors

Liu, Y.,Cheney, M.D.,Chruszcz, M.,Lukasik, S.M.,Hartman, K.L.,Laue, T.M.,Dauter, Z.,Minor, W.,Speck, N.A.,Bushweller, J.H. (deposition date: 2004-09-23, release date: 2005-10-04, Last modification date: 2024-10-23)

Primary citation

Liu, Y.,Cheney, M.D.,Gaudet, J.J.,Chruszcz, M.,Lukasik, S.M.,Sugiyama, D.,Lary, J.,Cole, J.,Dauter, Z.,Minor, W.,Speck, N.A.,Bushweller, J.H.
The tetramer structure of the Nervy homology two domain, NHR2, is critical for AML1/ETO's activity
Cancer Cell, 9:249-260, 2006

PubMed Abstract: AML1/ETO is the chimeric protein resulting from the t(8;21) in acute myeloid leukemia. The Nervy homology 2 (NHR2) domain in ETO mediates oligomerization and AML1/ETO's interactions with ETO, MTGR1, and MTG16, and with the corepressor molecules mSin3A and HDAC1 and HDAC3. We solved the NHR2 domain structure and found it to be an alpha-helical tetramer. We show that oligomerization contributes to AML1/ETO's inhibition of granulocyte differentiation, is essential for its ability to enhance the clonogenic potential of primary mouse bone marrow cells, and affects AML1/ETO's activity on several endogenous genes. Oligomerization is also required for AML1/ETO's interactions with ETO, MTGR1, and MTG16, but not with other corepressor molecules.

PubMed: 16616331
DOI: 10.1016/j.ccr.2006.03.012

Experimental method

X-RAY DIFFRACTION (2 Å)