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6y20

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Revision as of 13:17, 24 January 2024

Crystal structure of Protein Scalloped (222-440) bound to Protein Vestigial (298-337)

Structural highlights

6y20 is a 4 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.849Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SCAL_DROME Transcription factor which plays a key role in the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein Hippo (Hpo), in complex with its regulatory protein Salvador (Sav), phosphorylates and activates Warts (Wts) in complex with its regulatory protein Mats, which in turn phosphorylates and inactivates the Yorkie (Yki) oncoprotein. The Hippo/SWH signaling pathway inhibits the activity of the transcriptional complex formed by Scalloped (sd) and Yki and the target genes of this pathway include cyclin-E (cycE), diap1 and bantam. Sd promotes nuclear localization of Yki. Involved in the regulation of cell-specific gene expression during development, particularly in the differentiation of the nervous system. When in combination with vestigial (vg) it acts as a transcriptional activation complex that regulates gene expression in the wing. Binding to vg switches the DNA target selectivity of sd. Required autonomously for cell proliferation and viability within the wing blade. Required for proper sensory organ precursor (SOP) differentiation at the wing margin; required for correct expression of sens.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

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^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Liu X, Grammont M, Irvine KD. Roles for scalloped and vestigial in regulating cell affinity and interactions between the wing blade and the wing hinge. Dev Biol. 2000 Dec 15;228(2):287-303. PMID:11112330 doi:http://dx.doi.org/10.1006/dbio.2000.9939
↑ Srivastava A, Bell JB. Further developmental roles of the Vestigial/Scalloped transcription complex during wing development in Drosophila melanogaster. Mech Dev. 2003 May;120(5):587-96. PMID:12782275
↑ Zhang L, Ren F, Zhang Q, Chen Y, Wang B, Jiang J. The TEAD/TEF family of transcription factor Scalloped mediates Hippo signaling in organ size control. Dev Cell. 2008 Mar;14(3):377-87. doi: 10.1016/j.devcel.2008.01.006. Epub 2008 Feb , 7. PMID:18258485 doi:http://dx.doi.org/10.1016/j.devcel.2008.01.006
↑ Goulev Y, Fauny JD, Gonzalez-Marti B, Flagiello D, Silber J, Zider A. SCALLOPED interacts with YORKIE, the nuclear effector of the hippo tumor-suppressor pathway in Drosophila. Curr Biol. 2008 Mar 25;18(6):435-41. doi: 10.1016/j.cub.2008.02.034. Epub 2008 , Feb 28. PMID:18313299 doi:http://dx.doi.org/10.1016/j.cub.2008.02.034
↑ Simmonds AJ, Liu X, Soanes KH, Krause HM, Irvine KD, Bell JB. Molecular interactions between Vestigial and Scalloped promote wing formation in Drosophila. Genes Dev. 1998 Dec 15;12(24):3815-20. PMID:9869635
↑ Halder G, Polaczyk P, Kraus ME, Hudson A, Kim J, Laughon A, Carroll S. The Vestigial and Scalloped proteins act together to directly regulate wing-specific gene expression in Drosophila. Genes Dev. 1998 Dec 15;12(24):3900-9. PMID:9869643
↑ 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, Chène P. A new perspective on the interaction between the Vg/VGLL1-3 proteins and the TEAD transcription factors. Sci Rep. 2020 Oct 15;10(1):17442. PMID:33060790 doi:10.1038/s41598-020-74584-x

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6y20"

Categories: Drosophila melanogaster | Large Structures | Bokhovchuk F | Scheufler C | Villard F

@@ Line 1: / Line 1: @@
-====
+==Crystal structure of Protein Scalloped (222-440) bound to Protein Vestigial (298-337)==
-<StructureSection load='6y20' size='340' side='right'caption='[[6y20]]' scene=''>
+<StructureSection load='6y20' size='340' side='right'caption='[[6y20]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
+<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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6y20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y20 OCA], [http://pdbe.org/6y20 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6y20 RCSB], [http://www.ebi.ac.uk/pdbsum/6y20 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6y20 ProSAT]</span></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]] 1.849&#8491;</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/SCAL_DROME SCAL_DROME] Transcription factor which plays a key role in the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein Hippo (Hpo), in complex with its regulatory protein Salvador (Sav), phosphorylates and activates Warts (Wts) in complex with its regulatory protein Mats, which in turn phosphorylates and inactivates the Yorkie (Yki) oncoprotein. The Hippo/SWH signaling pathway inhibits the activity of the transcriptional complex formed by Scalloped (sd) and Yki and the target genes of this pathway include cyclin-E (cycE), diap1 and bantam. Sd promotes nuclear localization of Yki. Involved in the regulation of cell-specific gene expression during development, particularly in the differentiation of the nervous system. When in combination with vestigial (vg) it acts as a transcriptional activation complex that regulates gene expression in the wing. Binding to vg switches the DNA target selectivity of sd. Required autonomously for cell proliferation and viability within the wing blade. Required for proper sensory organ precursor (SOP) differentiation at the wing margin; required for correct expression of sens.<ref>PMID:11112330</ref> <ref>PMID:12782275</ref> <ref>PMID:18258485</ref> <ref>PMID:18313299</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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 6y20" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
+[[Category: Drosophila melanogaster]]
 [[Category: Large Structures]]
-[[Category: Z-disk]]
+[[Category: Bokhovchuk F]]
+[[Category: Scheufler C]]
+[[Category: Villard F]]

6y20

From Proteopedia

Revision as of 13:17, 24 January 2024

Crystal structure of Protein Scalloped (222-440) bound to Protein Vestigial (298-337)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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