6Y20

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

6Y20 の概要

• エントリーDOI: 10.2210/pdb6y20/pdb
• 分子名称: Protein scalloped, Protein vestigial, MYRISTIC ACID, ... (5 entities in total)
• 機能のキーワード: complex, transcription
• 由来する生物種: Drosophila melanogaster (fruit fly); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 60775.81

構造登録者

Scheufler, C.,Villard, F.,Bokhovchuk, F. (登録日: 2020-02-14, 公開日: 2020-10-21, 最終更新日: 2024-05-29)

主引用文献

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.
A new perspective on the interaction between the Vg/VGLL1-3 proteins and the TEAD transcription factors.
Sci Rep, 10:17442-17442, 2020

PubMed Abstract: 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 Ω-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 Ω-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.

PubMed: 33060790
DOI: 10.1038/s41598-020-74584-x

実験手法

X-RAY DIFFRACTION (1.849 Å)