We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.
6y20
From Proteopedia
(Difference between revisions)
m (Protected "6y20" [edit=sysop:move=sysop]) |
|||
| (2 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Protein Scalloped (222-440) bound to Protein Vestigial (298-337)== | |
| + | <StructureSection load='6y20' size='340' side='right'caption='[[6y20]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6y20]] 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=6Y20 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Y20 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.849Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=MYK:N~6~-TETRADECANOYL-L-LYSINE'>MYK</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=6y20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y20 OCA], [https://pdbe.org/6y20 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6y20 RCSB], [https://www.ebi.ac.uk/pdbsum/6y20 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6y20 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/VG_DROME VG_DROME] Involved in determining which thoracic imaginal disk cells will form wings and halteres, perhaps by interacting with other nuclear regulatory proteins. When in combination with scalloped (sd), it acts as a transcriptional activation complex that regulates gene expression in the wing. Binding to sd switches the DNA target selectivity of sd. Required and sufficient for cell proliferation at the dorsal/ventral (D/V) boundary of the wing imaginal disk. Also required for cell proliferation in the wing imaginal disk, mediated via activation of E2f. By interacting with Dhfr, may control genes involved in DNA replication.<ref>PMID:14526388</ref> <ref>PMID:1752439</ref> <ref>PMID:9869635</ref> <ref>PMID:9869643</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The most downstream elements of the Hippo pathway, the TEAD transcription factors, are regulated by several cofactors, such as Vg/VGLL1-3. Earlier findings on human VGLL1 and here on human VGLL3 show that these proteins interact with TEAD via a conserved amino acid motif called the TONDU domain. Surprisingly, our studies reveal that the TEAD-binding domain of Drosophila Vg and of human VGLL2 is more complex and contains an additional structural element, an Omega-loop, that contributes to TEAD binding. To explain this unexpected structural difference between proteins from the same family, we propose that, after the genome-wide duplications at the origin of vertebrates, the Omega-loop present in an ancestral VGLL gene has been lost in some VGLL variants. These findings illustrate how structural and functional constraints can guide the evolution of transcriptional cofactors to preserve their ability to compete with other cofactors for binding to transcription factors. | ||
| - | + | A new perspective on the interaction between the Vg/VGLL1-3 proteins and the TEAD transcription factors.,Mesrouze Y, Aguilar G, Bokhovchuk F, Martin T, Delaunay C, Villard F, Meyerhofer M, Zimmermann C, Fontana P, Wille R, Vorherr T, Erdmann D, Furet P, Scheufler C, Schmelzle T, Affolter M, Chene P Sci Rep. 2020 Oct 15;10(1):17442. doi: 10.1038/s41598-020-74584-x. PMID:33060790<ref>PMID:33060790</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6y20" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Drosophila melanogaster]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bokhovchuk F]] | ||
| + | [[Category: Scheufler C]] | ||
| + | [[Category: Villard F]] | ||
Current revision
Crystal structure of Protein Scalloped (222-440) bound to Protein Vestigial (298-337)
| |||||||||||
