6fuz

Crystal structure of the TPR domain of KLC1 in complex with the C-terminal peptide of JIP1

spinqualitylabelsall models 6fuz, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6fuz is a 2 chain structure with sequence from Homo sapiens, Lama glama and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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(TPR)). 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(TPR) 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(TPR) with similar low micromolar affinity can exhibit different capacities to promote kinesin-1 activity. Structural basis for isoform-specific kinesin-1 recognition of Y-acidic cargo adaptors.,Pernigo S, Chegkazi MS, Yip YY, Treacy C, Glorani G, Hansen K, Politis A, Bui S, Dodding MP, Steiner RA Elife. 2018 Oct 15;7:e38362. doi: 10.7554/eLife.38362. PMID:30320553 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Kinesin 3D Structures

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