The crystal structure of the Dachshund domain of human SnoN reveals flexibility in the putative protein interaction surface.

ABSTRACT:

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The human SnoN is an oncoprotein that interacts with several transcription-regulatory proteins such as the histone-deacetylase, N-CoR containing co-repressor complex and Smad proteins. This study presents the crystal structure of the Dachshund homology domain of human SnoN. The structure reveals a groove composed of conserved residues with characteristic properties of a protein-interaction surface. A comparison of the 12 monomers in the asymmetric unit reveals the presence of two major conformations: an open conformation with a well accessible groove and a tight conformation with a less accessible groove. The variability in the backbone between the open and the tight conformations matches the differences seen in previously determined structures of individual Dachshund ho

SUBMITTER: Nyman T 

PROVIDER: S-EPMC2944819 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature