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2a90

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Revision as of 06:44, 9 May 2018

Crystal Structure of the tandem WWE domain of Drosophila Deltex

Structural highlights

2a90 is a 1 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:	dx (DROME)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DTX_DROME] Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. Mainly acts as a positive regulator of Notch, but it may also act as a negative regulator, depending on the developmental and cell context. Mediates the antineural activity of Notch. May function as a ubiquitin ligase protein in the Notch pathway.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Matsuno K, Diederich RJ, Go MJ, Blaumueller CM, Artavanis-Tsakonas S. Deltex acts as a positive regulator of Notch signaling through interactions with the Notch ankyrin repeats. Development. 1995 Aug;121(8):2633-44. PMID:7671825
↑ Ramain P, Khechumian K, Seugnet L, Arbogast N, Ackermann C, Heitzler P. Novel Notch alleles reveal a Deltex-dependent pathway repressing neural fate. Curr Biol. 2001 Nov 13;11(22):1729-38. PMID:11719214
↑ Matsuno K, Ito M, Hori K, Miyashita F, Suzuki S, Kishi N, Artavanis-Tsakonas S, Okano H. Involvement of a proline-rich motif and RING-H2 finger of Deltex in the regulation of Notch signaling. Development. 2002 Feb;129(4):1049-59. PMID:11861487
↑ Zweifel ME, Leahy DJ, Barrick D. Structure and Notch receptor binding of the tandem WWE domain of Deltex. Structure. 2005 Nov;13(11):1599-611. PMID:16271883 doi:10.1016/j.str.2005.07.015

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2a90"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of the tandem WWE domain of Drosophila Deltex==
 <StructureSection load='2a90' size='340' side='right' caption='[[2a90]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dx ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a90 OCA], [http://pdbe.org/2a90 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a90 RCSB], [http://www.ebi.ac.uk/pdbsum/2a90 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a90 OCA], [http://pdbe.org/2a90 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a90 RCSB], [http://www.ebi.ac.uk/pdbsum/2a90 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2a90 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a9/2a90_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a9/2a90_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2a90

From Proteopedia

Revision as of 06:44, 9 May 2018

Crystal Structure of the tandem WWE domain of Drosophila Deltex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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