1sbx
From Proteopedia
Crystal structure of the Dachshund-homology domain of human SKI
Contents |
Overview
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.
Disease
Known disease associated with this structure: 1p36 deletion syndrome OMIM:[164780]
About this Structure
1SBX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the dachshund homology domain of human SKI., Wilson JJ, Malakhova M, Zhang R, Joachimiak A, Hegde RS, Structure. 2004 May;12(5):785-92. PMID:15130471 Page seeded by OCA on Sat May 3 08:31:42 2008
