| Literature DB >> 15130471 |
Jeffrey J Wilson1, Margarita Malakhova, Rongguang Zhang, Andrzej Joachimiak, Rashmi S Hegde.
Abstract
The nuclear protooncoprotein SKI negatively regulates transforming growth factor-beta (TGF-beta) signaling in cell growth and differentiation. It directly interacts with the Smads and, by various mechanisms, represses the transcription of TGF-beta-responsive genes. SKI is a multidomain protein that includes a domain bearing high sequence similarity with the retinal determination protein Dachshund (the Dachshund homology domain, DHD). The SKI-DHD has been implicated in SMAD-2/3, N-CoR, SKIP, and PML-RARalpha binding. The 1.65 A crystal structure of the Dachshund homology domain of human SKI is reported here. The SKI-DHD adopts a mixed alpha/beta structure which includes features found in the forkhead/winged-helix family of DNA binding proteins, although SKI-DHD is not a DNA binding domain. Residues that form a contiguous surface patch on SKI-DHD are conserved within the Ski/Sno family and with Dachshund, suggesting that this domain may mediate intermolecular interactions common to these proteins.Entities:
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Year: 2004 PMID： 15130471 DOI： 10.1016/j.str.2004.02.035
Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006