5NR4
Crystal structure of Clasp2 TOG1 domain
5NR4 の概要
| エントリーDOI | 10.2210/pdb5nr4/pdb |
| 分子名称 | CLIP-associating protein 2 (2 entities in total) |
| 機能のキーワード | microtubules, tog domain, tubulin, structural protein |
| 由来する生物種 | Homo sapiens (Human) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 51508.13 |
| 構造登録者 | Sharma, A.,Olieric, N.,Weinert, T.,Olieric, V.,Steinmetz, M.O. (登録日: 2017-04-21, 公開日: 2018-05-30, 最終更新日: 2024-05-08) |
| 主引用文献 | Aher, A.,Kok, M.,Sharma, A.,Rai, A.,Olieric, N.,Rodriguez-Garcia, R.,Katrukha, E.A.,Weinert, T.,Olieric, V.,Kapitein, L.C.,Steinmetz, M.O.,Dogterom, M.,Akhmanova, A. CLASP Suppresses Microtubule Catastrophes through a Single TOG Domain. Dev. Cell, 46:40-58.e8, 2018 Cited by PubMed Abstract: The dynamic instability of microtubules plays a key role in controlling their organization and function, but the cellular mechanisms regulating this process are poorly understood. Here, we show that cytoplasmic linker-associated proteins (CLASPs) suppress transitions from microtubule growth to shortening, termed catastrophes, including those induced by microtubule-destabilizing agents and physical barriers. Mammalian CLASPs encompass three TOG-like domains, TOG1, TOG2, and TOG3, none of which bind to free tubulin. TOG2 is essential for catastrophe suppression, whereas TOG3 mildly enhances rescues but cannot suppress catastrophes. These functions are inhibited by the C-terminal domain of CLASP2, while the TOG1 domain can release this auto-inhibition. TOG2 fused to a positively charged microtubule-binding peptide autonomously accumulates at growing but not shrinking ends, suppresses catastrophes, and stimulates rescues. CLASPs suppress catastrophes by stabilizing growing microtubule ends, including incomplete ones, preventing their depolymerization and promoting their recovery into complete tubes. TOG2 domain is the key determinant of these activities. PubMed: 29937387DOI: 10.1016/j.devcel.2018.05.032 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.198 Å) |
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