6GVM
Tubulin:F3II DARPin complex
6GVM の概要
| エントリーDOI | 10.2210/pdb6gvm/pdb |
| 分子名称 | Tubulin alpha chain, Tubulin beta chain, STATHMIN-LIKE DOMAIN R1, ... (7 entities in total) |
| 機能のキーワード | microtubule, darpin, stathmin-like protein, cell cycle |
| 由来する生物種 | Ovis aries (Sheep) 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 129563.94 |
| 構造登録者 | Gigant, B.,Campanacci, V.,Cantos Fernandes, S. (登録日: 2018-06-21, 公開日: 2019-04-24, 最終更新日: 2024-01-17) |
| 主引用文献 | Campanacci, V.,Urvoas, A.,Cantos-Fernandes, S.,Aumont-Nicaise, M.,Arteni, A.A.,Velours, C.,Valerio-Lepiniec, M.,Dreier, B.,Pluckthun, A.,Pilon, A.,Pous, C.,Minard, P.,Gigant, B. Insight into microtubule nucleation from tubulin-capping proteins. Proc.Natl.Acad.Sci.USA, 116:9859-9864, 2019 Cited by PubMed Abstract: Nucleation is one of the least understood steps of microtubule dynamics. It is a kinetically unfavorable process that is templated in the cell by the γ-tubulin ring complex or by preexisting microtubules; it also occurs in vitro from pure tubulin. Here we study the nucleation inhibition potency of natural or artificial proteins in connection with their binding mode to the longitudinal surface of α- or β-tubulin. The structure of tubulin-bound CopN, a protein that delays nucleation, suggests that this protein may interfere with two protofilaments at the (+) end of a nucleus. Designed ankyrin repeat proteins that share a binding mode similar to that of CopN also impede nucleation, whereas those that target only one protofilament do not. In addition, an αRep protein predicted to target two protofilaments at the (-) end does not delay nucleation, pointing to different behaviors at both ends of the nucleus. Our results link the interference with protofilaments at the (+) end and the inhibition of nucleation. PubMed: 31036638DOI: 10.1073/pnas.1813559116 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.5 Å) |
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