1SBX

Crystal structure of the Dachshund-homology domain of human SKI

Summary for 1SBX

• Entry DOI: 10.2210/pdb1sbx/pdb
• Descriptor: Ski oncogene (2 entities in total)
• Functional Keywords: winged helix, forkhead, oncoprotein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P12755
• Total number of polymer chains: 1
• Total formula weight: 11867.27

Authors

Wilson, J.J.,Malakhova, M.,Zhang, R.,Joachimiak, A.,Hegde, R.S. (deposition date: 2004-02-11, release date: 2004-05-25, Last modification date: 2024-10-30)

Primary citation

Wilson, J.J.,Malakhova, M.,Zhang, R.,Joachimiak, A.,Hegde, R.S.
Crystal Structure of the Dachshund Homology Domain of human SKI
Structure, 12:785-792, 2004

PubMed 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.

PubMed: 15130471
DOI: 10.1016/j.str.2004.02.035

Experimental method

X-RAY DIFFRACTION (1.65 Å)