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==Crystal structure of the TPR domain of KLC1 in complex with the C-terminal peptide of JIP1== | ==Crystal structure of the TPR domain of KLC1 in complex with the C-terminal peptide of JIP1== | ||
<StructureSection load='6fuz' size='340' side='right' caption='[[6fuz]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='6fuz' size='340' side='right'caption='[[6fuz]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6fuz]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6fuz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Lama_glama Lama glama] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FUZ FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6fuz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fuz OCA], [https://pdbe.org/6fuz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fuz RCSB], [https://www.ebi.ac.uk/pdbsum/6fuz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fuz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == 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 | 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<ref>PMID:30320553</ref> | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 6fuz" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6fuz" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Kinesin 3D Structures|Kinesin 3D Structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Lama]] | [[Category: Lama glama]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: | [[Category: Dodding MP]] | ||
[[Category: | [[Category: Pernigo S]] | ||
[[Category: | [[Category: Steiner RA]] | ||
Latest revision as of 10:58, 17 October 2024
Crystal structure of the TPR domain of KLC1 in complex with the C-terminal peptide of JIP1Crystal structure of the TPR domain of KLC1 in complex with the C-terminal peptide of JIP1
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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