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3THF

Crystal structure of the SD2 domain from Drosophila Shroom

3THF の概要
エントリーDOI10.2210/pdb3thf/pdb
分子名称Protein Shroom (1 entity in total)
機能のキーワードcoiled-coil, anti-parallel, helical, rho-kinase, actin-binding, protein binding, cytoskeleton regulator, actin-binding protein-protein binding complex, actin-binding protein/protein binding
由来する生物種Drosophila melanogaster (Fruit fly)
細胞内の位置Cytoplasm, cytoskeleton: A1Z9P3
タンパク質・核酸の鎖数2
化学式量合計42748.36
構造登録者
Mohan, S.,VanDemark, A.P. (登録日: 2011-08-18, 公開日: 2012-06-06, 最終更新日: 2024-02-28)
主引用文献Mohan, S.,Rizaldy, R.,Das, D.,Bauer, R.J.,Heroux, A.,Trakselis, M.A.,Hildebrand, J.D.,VanDemark, A.P.
Structure of Shroom domain 2 reveals a three-segmented coiled-coil required for dimerization, Rock binding, and apical constriction.
Mol Biol Cell, 23:2131-2142, 2012
Cited by
PubMed Abstract: Shroom (Shrm) proteins are essential regulators of cell shape and tissue morpho-logy during animal development that function by interacting directly with the coiled-coil region of Rho kinase (Rock). The Shrm-Rock interaction is sufficient to direct Rock subcellular localization and the subsequent assembly of contractile actomyosin networks in defined subcellular locales. However, it is unclear how the Shrm-Rock interaction is regulated at the molecular level. To begin investigating this issue, we present the structure of Shrm domain 2 (SD2), which mediates the interaction with Rock and is required for Shrm function. SD2 is a unique three-segmented dimer with internal symmetry, and we identify conserved residues on the surface and within the dimerization interface that are required for the Rock-Shrm interaction and Shrm activity in vivo. We further show that these residues are critical in both vertebrate and invertebrate Shroom proteins, indicating that the Shrm-Rock signaling module has been functionally and molecularly conserved. The structure and biochemical analysis of Shrm SD2 indicate that it is distinct from other Rock activators such as RhoA and establishes a new paradigm for the Rock-mediated assembly of contractile actomyosin networks.
PubMed: 22493320
DOI: 10.1091/mbc.E11-11-0937
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.6951 Å)
構造検証レポート
Validation report summary of 3thf
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-28に公開中

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