2OD1

Solution structure of the MYND domain from human AML1-ETO

Summary for 2OD1

• Entry DOI: 10.2210/pdb2od1/pdb
• Descriptor: Protein CBFA2T1, ZINC ION (2 entities in total)
• Functional Keywords: zinc finger, cross-braced topology, metal binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus (Potential): Q06455
• Total number of polymer chains: 1
• Total formula weight: 6672.86

Authors

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. (deposition date: 2006-12-21, release date: 2007-06-19, Last modification date: 2023-12-27)

Primary citation

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

Experimental method

SOLUTION NMR