2a90
From Proteopedia
(New page: 200px<br /><applet load="2a90" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a90, resolution 2.150Å" /> '''Crystal Structure o...) |
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- | [[Image:2a90.gif|left|200px]]<br /><applet load="2a90" size=" | + | [[Image:2a90.gif|left|200px]]<br /><applet load="2a90" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2a90, resolution 2.150Å" /> | caption="2a90, resolution 2.150Å" /> | ||
'''Crystal Structure of the tandem WWE domain of Drosophila Deltex'''<br /> | '''Crystal Structure of the tandem WWE domain of Drosophila Deltex'''<br /> | ||
==Overview== | ==Overview== | ||
- | Deltex is a cytosolic effector of Notch signaling thought to bind through | + | Deltex is a cytosolic effector of Notch signaling thought to bind through its N-terminal domain to the Notch receptor. Here we report the structure of the Drosophila Deltex N-terminal domain, which contains two tandem WWE sequence repeats. The WWE repeats, which adopt a novel fold, are related by an approximate two-fold axis of rotation. Although the WWE repeats are structurally distinct, they interact extensively and form a deep cleft at their junction that appears well suited for ligand binding. The two repeats are thermodynamically coupled; this coupling is mediated in part by a conserved segment that is immediately C-terminal to the second WWE domain. We demonstrate that although the Deltex WWE tandem is monomeric in solution, it forms a heterodimer with the ankyrin domain of the Notch receptor. These results provide structural and functional insight into how Deltex modulates Notch signaling, and how WWE modules recognize targets for ubiquitination. |
==About this Structure== | ==About this Structure== | ||
- | 2A90 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http:// | + | 2A90 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A90 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Barrick, D.]] | [[Category: Barrick, D.]] | ||
- | [[Category: Leahy, D | + | [[Category: Leahy, D J.]] |
- | [[Category: Zweifel, M | + | [[Category: Zweifel, M E.]] |
[[Category: wwe domain]] | [[Category: wwe domain]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:24:55 2008'' |
Revision as of 14:24, 21 February 2008
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Crystal Structure of the tandem WWE domain of Drosophila Deltex
Overview
Deltex is a cytosolic effector of Notch signaling thought to bind through its N-terminal domain to the Notch receptor. Here we report the structure of the Drosophila Deltex N-terminal domain, which contains two tandem WWE sequence repeats. The WWE repeats, which adopt a novel fold, are related by an approximate two-fold axis of rotation. Although the WWE repeats are structurally distinct, they interact extensively and form a deep cleft at their junction that appears well suited for ligand binding. The two repeats are thermodynamically coupled; this coupling is mediated in part by a conserved segment that is immediately C-terminal to the second WWE domain. We demonstrate that although the Deltex WWE tandem is monomeric in solution, it forms a heterodimer with the ankyrin domain of the Notch receptor. These results provide structural and functional insight into how Deltex modulates Notch signaling, and how WWE modules recognize targets for ubiquitination.
About this Structure
2A90 is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
Structure and Notch receptor binding of the tandem WWE domain of Deltex., Zweifel ME, Leahy DJ, Barrick D, Structure. 2005 Nov;13(11):1599-611. PMID:16271883
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