6ZPH

Kinesin binding protein complexed with Kif15 motor domain

6ZPH の概要

• エントリーDOI: 10.2210/pdb6zph/pdb
• 関連するPDBエントリー: 6ZPG
• EMDBエントリー: 11338 11339
• 分子名称: KIF-binding protein, Kinesin-like protein KIF15, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: kinesin, microtubules, kinesin binding protein, kbp, motor protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 114351.46

構造登録者

Atherton, J.,Hummel, J.J.A.,Olieric, N.,Locke, J.,Pena, A.,Rosenfeld, S.S.,Steinmetz, M.O.,Hoogenraad, C.C.,Moores, C.A. (登録日: 2020-07-08, 公開日: 2020-12-30, 最終更新日: 2024-05-01)

主引用文献

Atherton, J.,Hummel, J.J.,Olieric, N.,Locke, J.,Pena, A.,Rosenfeld, S.S.,Steinmetz, M.O.,Hoogenraad, C.C.,Moores, C.A.
The mechanism of kinesin inhibition by kinesin-binding protein.
Elife, 9:-, 2020

PubMed Abstract: Subcellular compartmentalisation is necessary for eukaryotic cell function. Spatial and temporal regulation of kinesin activity is essential for building these local environments via control of intracellular cargo distribution. Kinesin-binding protein (KBP) interacts with a subset of kinesins via their motor domains, inhibits their microtubule (MT) attachment, and blocks their cellular function. However, its mechanisms of inhibition and selectivity have been unclear. Here we use cryo-electron microscopy to reveal the structure of KBP and of a KBP-kinesin motor domain complex. KBP is a tetratricopeptide repeat-containing, right-handed α-solenoid that sequesters the kinesin motor domain's tubulin-binding surface, structurally distorting the motor domain and sterically blocking its MT attachment. KBP uses its α-solenoid concave face and edge loops to bind the kinesin motor domain, and selected structure-guided mutations disrupt KBP inhibition of kinesin transport in cells. The KBP-interacting motor domain surface contains motifs exclusively conserved in KBP-interacting kinesins, suggesting a basis for kinesin selectivity.

PubMed: 33252036
DOI: 10.7554/eLife.61481

実験手法

ELECTRON MICROSCOPY (6.9 Å)