7C1M
Complex structure of tyrosinated alpha-tubulin carboxy-terminal peptide and A1aY1 binder
7C1M の概要
| エントリーDOI | 10.2210/pdb7c1m/pdb |
| NMR情報 | BMRB: 36353 |
| 分子名称 | Nanobody binder from SSO7d library, Carboxy-terminal peptide from tyrosinated alpha-tubulin (2 entities in total) |
| 機能のキーワード | tyrosinated, microtubule, binder, sso7d, yeast display, protein binding |
| 由来する生物種 | Saccharolobus solfataricus 98/2 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 8842.13 |
| 構造登録者 | Kesarwani, S.,Reddy, P.P.,Sirajuddin, M.,Das, R. (登録日: 2020-05-05, 公開日: 2020-09-02, 最終更新日: 2024-05-15) |
| 主引用文献 | Kesarwani, S.,Lama, P.,Chandra, A.,Reddy, P.P.,Jijumon, A.S.,Bodakuntla, S.,Rao, B.M.,Janke, C.,Das, R.,Sirajuddin, M. Genetically encoded live-cell sensor for tyrosinated microtubules. J.Cell Biol., 219:-, 2020 Cited by PubMed Abstract: Microtubule cytoskeleton exists in various biochemical forms in different cells due to tubulin posttranslational modifications (PTMs). Tubulin PTMs are known to affect microtubule stability, dynamics, and interaction with MAPs and motors in a specific manner, widely known as tubulin code hypothesis. At present, there exists no tool that can specifically mark tubulin PTMs in living cells, thus severely limiting our understanding of their dynamics and cellular functions. Using a yeast display library, we identified a binder against terminal tyrosine of α-tubulin, a unique PTM site. Extensive characterization validates the robustness and nonperturbing nature of our binder as tyrosination sensor, a live-cell tubulin nanobody specific towards tyrosinated microtubules. Using this sensor, we followed nocodazole-, colchicine-, and vincristine-induced depolymerization events of tyrosinated microtubules in real time and found each distinctly perturbs the microtubule polymer. Together, our work describes a novel tyrosination sensor and its potential applications to study the dynamics of microtubule and their PTM processes in living cells. PubMed: 32886100DOI: 10.1083/jcb.201912107 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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