View source for 5fjy


==Crystal structure of mouse kinesin light chain 2 (residues 161-480)==
<StructureSection load='5fjy' size='340' side='right'caption='[[5fjy]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5fjy]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FJY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FJY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fjy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fjy OCA], [https://pdbe.org/5fjy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fjy RCSB], [https://www.ebi.ac.uk/pdbsum/5fjy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fjy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KLC2_MOUSE KLC2_MOUSE] Kinesin is a microtubule-associated force-producing protein that plays a role in organelle transport. The light chain functions in coupling of cargo to the heavy chain or in the modulation of its ATPase activity. Through binding with PLEKHM2 and ARL8B, recruits kinesin-1 to lysosomes and hence direct lysosomes movement toward microtubule plus ends.[UniProtKB:Q9H0B6]
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== Publication Abstract from PubMed ==
The light chains (KLCs) of the microtubule motor kinesin-1 bind cargoes and regulate its activity. Through their tetratricopeptide repeat domain (KLCTPR), they can recognize short linear peptide motifs found in many cargo proteins characterized by a central tryptophan flanked by aspartic/glutamic acid residues (W-acidic). Using a fluorescence resonance energy transfer biosensor in combination with X-ray crystallographic, biochemical, and biophysical approaches, we describe how an intramolecular interaction between the KLC2TPR domain and a conserved peptide motif within an unstructured region of the molecule, partly occludes the W-acidic binding site on the TPR domain. Cargo binding displaces this interaction, effecting a global conformational change in KLCs resulting in a more extended conformation. Thus, like the motor-bearing kinesin heavy chains, KLCs exist in a dynamic conformational state that is regulated by self-interaction and cargo binding. We propose a model by which, via this molecular switch, W-acidic cargo binding regulates the activity of the holoenzyme.

The light chains of kinesin-1 are autoinhibited.,Yip YY, Pernigo S, Sanger A, Xu M, Parsons M, Steiner RA, Dodding MP Proc Natl Acad Sci U S A. 2016 Feb 16. pii: 201520817. PMID:26884162<ref>PMID:26884162</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5fjy" style="background-color:#fffaf0;"></div>

==See Also==
*[[Kinesin 3D Structures|Kinesin 3D Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Dodding MP]]
[[Category: Pernigo S]]
[[Category: Sanger A]]
[[Category: Steiner RA]]
[[Category: Xu M]]
[[Category: Yip YY]]