2OD1: Solution structure of the MYND domain from human AML1-ETO

Citation:
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.
PDB ID: 2OD1Download
MMDB ID: 46927
PDB Deposition Date: 2006/12/21
Updated in MMDB: 2012/12
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Molecular Components in 2OD1
Label Count Molecule
Protein (1 molecule)
1
Protein Cbfa2t1(Gene symbol: RUNX1T1)
Molecule annotation
Chemicals (2 molecules)
1
2
* Click molecule labels to explore molecular sequence information.

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