6FV0

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

Summary for 6FV0

• Entry DOI: 10.2210/pdb6fv0/pdb
• Descriptor: Kinesin light chain 1,Torsin-1A, nanobody, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• Functional Keywords: protein complex, motor protein, nanobody, cargo recognition
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 2
• Total formula weight: 50950.93

Authors

Pernigo, S.,Dodding, M.P.,Steiner, R.A. (deposition date: 2018-02-28, release date: 2018-03-28, Last modification date: 2024-11-06)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.29 Å)