3NRX

Insights into anti-parallel microtubule crosslinking by PRC1, a conserved non-motor microtubule binding protein

3NRX の概要

• エントリーDOI: 10.2210/pdb3nrx/pdb
• 関連するPDBエントリー: 3NRY
• 分子名称: Protein regulator of cytokinesis 1 (2 entities in total)
• 機能のキーワード: spectrin fold, microtubule binding domain, protein binding
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: O43663
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31676.14

構造登録者

Kapoor, T.M.,Subramanian, R.,Wilson-Kubalek, E.M.,Arthur, C.P.,Bick, M.J.,Campbell, E.A.,Darst, S.A.,Milligan, R.A. (登録日: 2010-06-30, 公開日: 2010-08-18, 最終更新日: 2023-09-06)

主引用文献

Subramanian, R.,Wilson-Kubalek, E.M.,Arthur, C.P.,Bick, M.J.,Campbell, E.A.,Darst, S.A.,Milligan, R.A.,Kapoor, T.M.
Insights into Antiparallel Microtubule Crosslinking by PRC1, a Conserved Nonmotor Microtubule Binding Protein.
Cell(Cambridge,Mass.), 142:433-443, 2010

PubMed Abstract: Formation of microtubule architectures, required for cell shape maintenance in yeast, directional cell expansion in plants and cytokinesis in eukaryotes, depends on antiparallel microtubule crosslinking by the conserved MAP65 protein family. Here, we combine structural and single molecule fluorescence methods to examine how PRC1, the human MAP65, crosslinks antiparallel microtubules. We find that PRC1's microtubule binding is mediated by a structured domain with a spectrin-fold and an unstructured Lys/Arg-rich domain. These two domains, at each end of a homodimer, are connected by a linkage that is flexible on single microtubules, but forms well-defined crossbridges between antiparallel filaments. Further, we show that PRC1 crosslinks are compliant and do not substantially resist filament sliding by motor proteins in vitro. Together, our data show how MAP65s, by combining structural flexibility and rigidity, tune microtubule associations to establish crosslinks that selectively "mark" antiparallel overlap in dynamic cytoskeletal networks.

PubMed: 20691902
DOI: 10.1016/j.cell.2010.07.012

実験手法

X-RAY DIFFRACTION (1.75 Å)