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| | ==Crystal structure of DM14-3 domain of Lgd== | | ==Crystal structure of DM14-3 domain of Lgd== |
| - | <StructureSection load='5vny' size='340' side='right' caption='[[5vny]], [[Resolution|resolution]] 1.10Å' scene=''> | + | <StructureSection load='5vny' size='340' side='right'caption='[[5vny]], [[Resolution|resolution]] 1.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5vny]] is a 1 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=5VNY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VNY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5vny]] is a 1 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=5VNY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VNY FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.101Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">l(2)gd1, CG4713, Dmel_CG4713 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5vny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vny OCA], [http://pdbe.org/5vny PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vny RCSB], [http://www.ebi.ac.uk/pdbsum/5vny PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vny 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=5vny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vny OCA], [https://pdbe.org/5vny PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vny RCSB], [https://www.ebi.ac.uk/pdbsum/5vny PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vny ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/C2D1_DROME C2D1_DROME] Negative regulator of the Notch signaling pathway, acting to restrict the activity of Notch to the dorsoventral (D/V) boundary of the wing imaginal disk. Also causes negative regulation of Notch during vein, eye, and bristle development. Acts by targeting Notch for endosomal degradation or recycling.<ref>PMID:12648493</ref> <ref>PMID:17088062</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| - | [[Category: Blacklow, S C]] | + | [[Category: Large Structures]] |
| - | [[Category: McMillan, B J]] | + | [[Category: Blacklow SC]] |
| - | [[Category: Endocytosis]] | + | [[Category: McMillan BJ]] |
| - | [[Category: Escrt]]
| + | |
| - | [[Category: Protein binding]]
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| Structural highlights
Function
C2D1_DROME Negative regulator of the Notch signaling pathway, acting to restrict the activity of Notch to the dorsoventral (D/V) boundary of the wing imaginal disk. Also causes negative regulation of Notch during vein, eye, and bristle development. Acts by targeting Notch for endosomal degradation or recycling.[1] [2]
Publication Abstract from PubMed
The ESCRT-III complex induces outward membrane budding and fission through homotypic polymerization of its core component Shrub/CHMP4B. Shrub activity is regulated by its direct interaction with a protein called Lgd in flies, or CC2D1A or B in humans. Here, we report the structural basis for this interaction and propose a mechanism for regulation of polymer assembly. The isolated third DM14 repeat of Lgd binds Shrub, and an Lgd fragment containing only this DM14 repeat and its C-terminal C2 domain is sufficient for in vivo function. The DM14 domain forms a helical hairpin with a conserved, positively charged tip, that, in the structure of a DM14 domain-Shrub complex, occupies a negatively charged surface of Shrub that is otherwise used for homopolymerization. Lgd mutations at this interface disrupt its function in flies, confirming functional importance. Together, these data argue that Lgd regulates ESCRT activity by controlling access to the Shrub self-assembly surface.
Structural Basis for Regulation of ESCRT-III Complexes by Lgd.,McMillan BJ, Tibbe C, Drabek AA, Seegar TCM, Blacklow SC, Klein T Cell Rep. 2017 May 30;19(9):1750-1757. doi: 10.1016/j.celrep.2017.05.026. PMID:28564595[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Klein T. The tumour suppressor gene l(2)giant discs is required to restrict the activity of Notch to the dorsoventral boundary during Drosophila wing development. Dev Biol. 2003 Mar 15;255(2):313-33. PMID:12648493
- ↑ Childress JL, Acar M, Tao C, Halder G. Lethal giant discs, a novel C2-domain protein, restricts notch activation during endocytosis. Curr Biol. 2006 Nov 21;16(22):2228-33. Epub 2006 Nov 9. PMID:17088062 doi:http://dx.doi.org/S0960-9822(06)02224-X
- ↑ McMillan BJ, Tibbe C, Drabek AA, Seegar TCM, Blacklow SC, Klein T. Structural Basis for Regulation of ESCRT-III Complexes by Lgd. Cell Rep. 2017 May 30;19(9):1750-1757. doi: 10.1016/j.celrep.2017.05.026. PMID:28564595 doi:http://dx.doi.org/10.1016/j.celrep.2017.05.026
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