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1mr1

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(New page: 200px<br /> <applet load="1mr1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mr1, resolution 2.85&Aring;" /> '''Crystal Structure o...)
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[[Image:1mr1.gif|left|200px]]<br />
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[[Image:1mr1.gif|left|200px]]<br /><applet load="1mr1" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1mr1" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1mr1, resolution 2.85&Aring;" />
caption="1mr1, resolution 2.85&Aring;" />
'''Crystal Structure of a Smad4-Ski Complex'''<br />
'''Crystal Structure of a Smad4-Ski Complex'''<br />
==Overview==
==Overview==
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The Ski family of nuclear oncoproteins represses TGF-beta signaling, through interactions with the Smad proteins. The crystal structure of the, Smad4 binding domain of human c-Ski in complex with the MH2 domain of, Smad4 reveals specific recognition of the Smad4 L3 loop region by a highly, conserved interaction loop (I loop) from Ski. The Ski binding surface on, Smad4 significantly overlaps with that required for binding of the, R-Smads. Indeed, Ski disrupts the formation of a functional complex, between the Co- and R-Smads, explaining how it could lead to repression of, TGF-beta, activin, and BMP responses. Intriguingly, the structure of the, Ski fragment, stabilized by a bound zinc atom, resembles the SAND domain, in which the corresponding I loop is responsible for DNA binding.
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The Ski family of nuclear oncoproteins represses TGF-beta signaling through interactions with the Smad proteins. The crystal structure of the Smad4 binding domain of human c-Ski in complex with the MH2 domain of Smad4 reveals specific recognition of the Smad4 L3 loop region by a highly conserved interaction loop (I loop) from Ski. The Ski binding surface on Smad4 significantly overlaps with that required for binding of the R-Smads. Indeed, Ski disrupts the formation of a functional complex between the Co- and R-Smads, explaining how it could lead to repression of TGF-beta, activin, and BMP responses. Intriguingly, the structure of the Ski fragment, stabilized by a bound zinc atom, resembles the SAND domain, in which the corresponding I loop is responsible for DNA binding.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1MR1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MR1 OCA].
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1MR1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MR1 OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Chai, J.]]
[[Category: Chai, J.]]
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[[Category: Krawitz, A.R.]]
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[[Category: Krawitz, A R.]]
[[Category: Li, W.]]
[[Category: Li, W.]]
[[Category: Luo, K.]]
[[Category: Luo, K.]]
[[Category: Shi, Y.]]
[[Category: Shi, Y.]]
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[[Category: Wu, J.W.]]
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[[Category: Wu, J W.]]
[[Category: Zhang, F.]]
[[Category: Zhang, F.]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: tgf-b signaling]]
[[Category: tgf-b signaling]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:14:15 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:12 2008''

Revision as of 11:58, 21 February 2008


1mr1, resolution 2.85Å

Drag the structure with the mouse to rotate

Crystal Structure of a Smad4-Ski Complex

Contents

Overview

The Ski family of nuclear oncoproteins represses TGF-beta signaling through interactions with the Smad proteins. The crystal structure of the Smad4 binding domain of human c-Ski in complex with the MH2 domain of Smad4 reveals specific recognition of the Smad4 L3 loop region by a highly conserved interaction loop (I loop) from Ski. The Ski binding surface on Smad4 significantly overlaps with that required for binding of the R-Smads. Indeed, Ski disrupts the formation of a functional complex between the Co- and R-Smads, explaining how it could lead to repression of TGF-beta, activin, and BMP responses. Intriguingly, the structure of the Ski fragment, stabilized by a bound zinc atom, resembles the SAND domain, in which the corresponding I loop is responsible for DNA binding.

Disease

Known diseases associated with this structure: 1p36 deletion syndrome OMIM:[164780], Juvenile polyposis/hereditary hemorrhagic telangiectasia syndrome OMIM:[600993], Pancreatic cancer OMIM:[600993], Polyposis, juvenile intestinal OMIM:[600993]

About this Structure

1MR1 is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Structural mechanism of Smad4 recognition by the nuclear oncoprotein Ski: insights on Ski-mediated repression of TGF-beta signaling., Wu JW, Krawitz AR, Chai J, Li W, Zhang F, Luo K, Shi Y, Cell. 2002 Nov 1;111(3):357-67. PMID:12419246

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