6FV0

Crystal structure of the TPR domain of KLC1 in complex with the C-terminal peptide of torsinA

6FV0 の概要

• エントリーDOI: 10.2210/pdb6fv0/pdb
• 分子名称: Kinesin light chain 1,Torsin-1A, nanobody, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• 機能のキーワード: protein complex, motor protein, nanobody, cargo recognition
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 50950.93

構造登録者

Pernigo, S.,Dodding, M.P.,Steiner, R.A. (登録日: 2018-02-28, 公開日: 2018-03-28, 最終更新日: 2024-11-06)

主引用文献

Pernigo, S.,Chegkazi, M.S.,Yip, Y.Y.,Treacy, C.,Glorani, G.,Hansen, K.,Politis, A.,Bui, S.,Dodding, M.P.,Steiner, R.A.
Structural basis for isoform-specific kinesin-1 recognition of Y-acidic cargo adaptors.
Elife, 7:-, 2018

PubMed Abstract: The light chains (KLCs) of the heterotetrameric microtubule motor kinesin-1, that bind to cargo adaptor proteins and regulate its activity, have a capacity to recognize short peptides via their tetratricopeptide repeat domains (KLC). Here, using X-ray crystallography, we show how kinesin-1 recognizes a novel class of adaptor motifs that we call 'Y-acidic' (tyrosine flanked by acidic residues), in a KLC-isoform-specific manner. Binding specificities of Y-acidic motifs (present in JIP1 and in TorsinA) to KLC1 are distinct from those utilized for the recognition of W-acidic motifs, found in adaptors, that are KLC-isoform non-selective. However, a partial overlap on their receptor-binding sites implies that adaptors relying on Y-acidic and W-acidic motifs must act independently. We propose a model to explain why these two classes of motifs that bind to the concave surface of KLC with similar low micromolar affinity can exhibit different capacities to promote kinesin-1 activity.

PubMed: 30320553
DOI: 10.7554/eLife.38362

実験手法

X-RAY DIFFRACTION (2.29 Å)