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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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'''Crystal structure of the Dachshund-homology domain of human SKI'''<br />
'''Crystal structure of the Dachshund-homology domain of human SKI'''<br />
==Overview==
==Overview==
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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.
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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==
==Disease==
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==About this Structure==
==About this Structure==
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1SBX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SBX OCA].
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1SBX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SBX OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Hegde, R.S.]]
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[[Category: Hegde, R S.]]
[[Category: Joachimiak, A.]]
[[Category: Joachimiak, A.]]
[[Category: Malakhova, M.]]
[[Category: Malakhova, M.]]
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[[Category: Wilson, J.J.]]
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[[Category: Wilson, J J.]]
[[Category: Zhang, R.]]
[[Category: Zhang, R.]]
[[Category: forkhead]]
[[Category: forkhead]]
[[Category: winged helix]]
[[Category: winged helix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:12:17 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:59:55 2008''

Revision as of 12:59, 21 February 2008


1sbx, resolution 1.65Å

Drag the structure with the mouse to rotate

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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