4EJQ

Crystal structure of KIF1A C-CC1-FHA

4EJQ の概要

• エントリーDOI: 10.2210/pdb4ejq/pdb
• 関連するPDBエントリー: 4EGX
• 分子名称: Kinesin-like protein KIF1A (2 entities in total)
• 機能のキーワード: homodimer, fha domain, transport protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, cytoskeleton: Q12756
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 139029.00

構造登録者

Huo, L.,Yue, Y.,Ren, J.,Yu, J.,Liu, J.,Yu, Y.,Ye, F.,Xu, T.,Zhang, M.,Feng, W. (登録日: 2012-04-06, 公開日: 2012-10-03, 最終更新日: 2023-11-08)

主引用文献

Huo, L.,Yue, Y.,Ren, J.,Yu, J.,Liu, J.,Yu, Y.,Ye, F.,Xu, T.,Zhang, M.,Feng, W.
The CC1-FHA Tandem as a Central Hub for Controlling the Dimerization and Activation of Kinesin-3 KIF1A
Structure, 20:1550-1561, 2012

PubMed Abstract: Kinesin-3 KIF1A plays prominent roles in axonal transport and synaptogenesis. KIF1A adopts a monomeric form in vitro but acts as a processive dimer in vivo. The mechanism underlying the motor dimerization is poorly understood. Here, we find that the CC1-FHA tandem of KIF1A exists as a stable dimer. The structure of CC1-FHA reveals that the linker between CC1 and FHA unexpectedly forms a β-finger hairpin, which integrates CC1 with FHA assembling a CC1-FHA homodimer. More importantly, dissociation of the CC1-FHA dimer unleashes CC1 and the β-finger, which are both essential for the motor inhibition. Thus, dimerization of the CC1-FHA tandem not only promotes the KIF1A dimer formation but also may trigger the motor activity via sequestering the CC1/β-finger region. The CC1-FHA tandem likely functions as a hub for controlling the dimerization and activation of KIF1A, which may represent a new paradigm for the kinesin regulation shared by other kinesin-3 motors.

PubMed: 22863567
DOI: 10.1016/j.str.2012.07.002

実験手法

X-RAY DIFFRACTION (1.893 Å)