6y20

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

spinqualitylabelsall models 6y20, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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: ACE, MYK, MYR, NH2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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