1d2z
From Proteopedia
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<StructureSection load='1d2z' size='340' side='right'caption='[[1d2z]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1d2z' size='340' side='right'caption='[[1d2z]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1d2z]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1d2z]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D2Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D2Z FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1d2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d2z OCA], [https://pdbe.org/1d2z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d2z RCSB], [https://www.ebi.ac.uk/pdbsum/1d2z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d2z ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1d2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d2z OCA], [https://pdbe.org/1d2z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d2z RCSB], [https://www.ebi.ac.uk/pdbsum/1d2z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d2z ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/KPEL_DROME KPEL_DROME] Plays an essential role in the Tl receptor signaling pathway that establishes embryonic dorsoventral polarity; the signal directs import of dl into ventral and ventrolateral nuclei, thereby establishing dorsoventral polarity. Tub recruits pll to the plasma membrane and protein-protein interaction activates pll.<ref>PMID:8440018</ref> <ref>PMID:7527496</ref> <ref>PMID:7635064</ref> <ref>PMID:10330490</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1d2z ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1d2z ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The interaction of the serine/threonine kinase Pelle and adaptor protein Tube through their N-terminal death domains leads to the nuclear translocation of the transcription factor Dorsal and activation of zygotic patterning genes during Drosophila embryogenesis. Crystal structure of the Pelle and Tube death domain heterodimer reveals that the two death domains adopt a six-helix bundle fold and are arranged in an open-ended linear array with plastic interfaces mediating their interactions. The Tube death domain has an insertion between helices 2 and 3, and a C-terminal tail making significant and indispensable contacts in the heterodimer. In vivo assays of Pelle and Tube mutants confirmed that the integrity of the major heterodimer interface is critical to the activity of these molecules. | ||
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| - | Three-dimensional structure of a complex between the death domains of Pelle and Tube.,Xiao T, Towb P, Wasserman SA, Sprang SR Cell. 1999 Nov 24;99(5):545-55. PMID:10589682<ref>PMID:10589682</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1d2z" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Drosophila melanogaster]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Sprang | + | [[Category: Sprang SR]] |
| - | [[Category: Towb | + | [[Category: Towb P]] |
| - | [[Category: Wasserman | + | [[Category: Wasserman SA]] |
| - | [[Category: Xiao | + | [[Category: Xiao T]] |
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Current revision
THREE-DIMENSIONAL STRUCTURE OF A COMPLEX BETWEEN THE DEATH DOMAINS OF PELLE AND TUBE
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