RETRACTED: Structure and Functional Analysis of the MYND Domain

This article has been retracted at the request of the authors and the Editor-in-Chief. Please see Elsevier Policy on Article Withdrawal (http://www.elsevier.com/locate/withdrawalpolicy).

Reason: Following the publication of this article, the structures of three other MYND domains were deposited in the PDB (accession numbers 2D8Q, 2DJ8, 2OD1 [Liu, Y., Chen, W., Gaudet, J., Cheney, M.D., Roudaia, L., Cierpicki, T., Klet, R.C., Hartman, K., Laue, T.M., Speck, N.A., and Bushweller, J.H. (2007) 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]). These MYND domain structures all have a cross-brace topology for the two zinc binding sites, in contrast to the sequential topology that had been described. In light of these differences the authors re-checked their data and recorded additional NOE experiments, which have improved signal-to-noise and provide a number of crucial long-range NOE contacts that had not been observed previously. The new NOE data show that the DEAF1 MYND domain also adopts a cross-brace zinc coordination topology. The sequential zinc binding topology reported for the DEAF1 MYND domain is therefore incorrect. The Protein Data Bank (PDB) entry 2FV6 has been moved to the archive of obsolete PDB entries. The corrected structure of the DEAF1 MYND domain will be deposited in the Protein Data Bank, replacing the original entry.

The authors sincerely apologize for this error and any confusion it may have caused.

Despite the erroneous structure, the authors note that the biochemical and functional analyses of the BS69 MYND domain reported are not affected. The mutations that impair molecular interactions of the BS69 MYND domain map to N- and C-terminal residues flanking the MYND fold, and the characteristic electrostatic surface potential of the BS69 MYND homology model is largely unchanged when the new structure is used as a template. Thus, the conclusions drawn from the mutational analysis of BS69 in light of the distinct surface charge distribution remain valid.