3THF
Crystal structure of the SD2 domain from Drosophila Shroom
3THF の概要
| エントリーDOI | 10.2210/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 | |
| 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: 22493320DOI: 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) |
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