6B9H

Complex of Hook Domain with a Dynein Light Intermediate Chain Peptide

6B9H の概要

• エントリーDOI: 10.2210/pdb6b9h/pdb
• 分子名称: Protein Hook homolog 3, Cytoplasmic dynein 1 light intermediate chain 1 (3 entities in total)
• 機能のキーワード: dynein, dynactin, effector, hook, light intermediate chain (lic), protein transport-motor protein complex, protein transport/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: 21066.14

構造登録者

Lee, I.G.,Dominguez, R. (登録日: 2017-10-10, 公開日: 2018-03-21, 最終更新日: 2023-10-04)

主引用文献

Lee, I.G.,Olenick, M.A.,Boczkowska, M.,Franzini-Armstrong, C.,Holzbaur, E.L.F.,Dominguez, R.
A conserved interaction of the dynein light intermediate chain with dynein-dynactin effectors necessary for processivity.
Nat Commun, 9:986-986, 2018

PubMed Abstract: Cytoplasmic dynein is the major minus-end-directed microtubule-based motor in cells. Dynein processivity and cargo selectivity depend on cargo-specific effectors that, while generally unrelated, share the ability to interact with dynein and dynactin to form processive dynein-dynactin-effector complexes. How this is achieved is poorly understood. Here, we identify a conserved region of the dynein Light Intermediate Chain 1 (LIC1) that mediates interactions with unrelated dynein-dynactin effectors. Quantitative binding studies map these interactions to a conserved helix within LIC1 and to N-terminal fragments of Hook1, Hook3, BICD2, and Spindly. A structure of the LIC1 helix bound to the N-terminal Hook domain reveals a conformational change that creates a hydrophobic cleft for binding of the LIC1 helix. The LIC1 helix competitively inhibits processive dynein-dynactin-effector motility in vitro, whereas structure-inspired mutations in this helix impair lysosomal positioning in cells. The results reveal a conserved mechanism of effector interaction with dynein-dynactin necessary for processive motility.

PubMed: 29515126
DOI: 10.1038/s41467-018-03412-8

実験手法

X-RAY DIFFRACTION (1.5 Å)