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| <StructureSection load='1ik7' size='340' side='right'caption='[[1ik7]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1ik7' size='340' side='right'caption='[[1ik7]], [[Resolution|resolution]] 2.30Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1ik7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IK7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1IK7 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[1ik7]] is a 2 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=1IK7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IK7 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 2.3Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d2z|1d2z]]</td></tr>
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pelle ([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'>[https://proteopedia.org/fgij/fg.htm?mol=1ik7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ik7 OCA], [https://pdbe.org/1ik7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ik7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ik7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ik7 ProSAT]</span></td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1] </span></td></tr>
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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ik7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ik7 OCA], [http://pdbe.org/1ik7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ik7 RCSB], [http://www.ebi.ac.uk/pdbsum/1ik7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ik7 ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://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> | | [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=1ik7 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=1ik7 ConSurf]. |
| <div style="clear:both"></div> | | <div style="clear:both"></div> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The death domain (DD) of the protein kinase Pelle adopts a six-helix bundle fold in the crystal structure of the complex with its dimerization partner, Tube-DD. However, in crystals obtained from a solution of 45% 2-methyl-2,4-pentanediol (MPD), the C-terminal half of Pelle-DD folds into a single helix, and the N-terminal half of the molecule is disordered. The helical segment forms an antiparallel dimer with the corresponding helix of a symmetry-related molecule, and together they form extensive lattice interactions similar in number, composition, and buried surface to those in the six-helix bundle of the native fold. Secondary structure analysis by heteronuclear nuclear magnetic resonance spectroscopy (NMR) demonstrates that Pelle-DD adopts a six-helix bundle fold in aqueous solution. The fold is perturbed by MPD, with the largest chemical shift changes in one helix and two loop regions that encompass the Tube-DD binding site. Pelle-DD is stable to urea denaturation with a folding free energy of 7.9 kcal/mol at 25 degrees C but is destabilized, with loss of urea binding sites, in the presence of MPD. The data are consistent with a cosolvent denaturation model in which MPD denatures the N terminus of Pelle-DD but induces the C terminus to form a more compact structure and aggregate. A similar perturbation in vivo might occur at the plasma membrane and could have consequences for Pelle-mediated regulation. Generally, crystallographers should be aware that high concentrations of MPD or related cosolvents can alter the tertiary structure of susceptible proteins.
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| Cosolvent-induced transformation of a death domain tertiary structure.,Xiao T, Gardner KH, Sprang SR Proc Natl Acad Sci U S A. 2002 Aug 20;99(17):11151-6. Epub 2002 Aug 12. PMID:12177432<ref>PMID:12177432</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 1ik7" style="background-color:#fffaf0;"></div>
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| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Drome]] | | [[Category: Drosophila melanogaster]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Transferase]]
| | [[Category: Gardner KH]] |
| [[Category: Gardner, K H]] | | [[Category: Sprang SR]] |
| [[Category: Sprang, S R]] | | [[Category: Xiao T]] |
| [[Category: Xiao, T]] | |
| [[Category: Mpd crystallization]]
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| [[Category: Single helix]]
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| [[Category: Structural transition]]
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