5vny
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of DM14-3 domain of Lgd== | |
| + | <StructureSection load='5vny' size='340' side='right' caption='[[5vny]], [[Resolution|resolution]] 1.10Å' scene=''> | ||
| + | == 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> | ||
| + | </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">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='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> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:28564595</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5vny" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Drome]] | ||
| + | [[Category: Blacklow, S C]] | ||
| + | [[Category: McMillan, B J]] | ||
| + | [[Category: Endocytosis]] | ||
| + | [[Category: Escrt]] | ||
| + | [[Category: Protein binding]] | ||
Revision as of 10:05, 16 November 2017
Crystal structure of DM14-3 domain of Lgd
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