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1sbx

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(New page: 200px<br /> <applet load="1sbx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sbx, resolution 1.65&Aring;" /> '''Crystal structure o...)
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Revision as of 17:05, 12 November 2007

Image:1sbx.gif

1sbx, resolution 1.65Å

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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

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