5ojf: Difference between revisions
New page: '''Unreleased structure''' The entry 5ojf is ON HOLD until Paper Publication Authors: Nguyen, T.Q., Chenon, M., Vilela, F., Velours, C., Andreani, J., Fernandez-Varela, P., Llinas, P., ... |
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==Crystal Structure of KLC2-TPR domain (fragment [A1-B6]== | |||
<StructureSection load='5ojf' size='340' side='right'caption='[[5ojf]], [[Resolution|resolution]] 3.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ojf]] is a 3 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=5OJF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OJF 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]] 3.4Å</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=5ojf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ojf OCA], [https://pdbe.org/5ojf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ojf RCSB], [https://www.ebi.ac.uk/pdbsum/5ojf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ojf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q91YS4_MOUSE Q91YS4_MOUSE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Kinesin1 plays a major role in neuronal transport by recruiting many different cargos through its kinesin light chain (KLC). Various structurally unrelated cargos interact with the conserved tetratricopeptide repeat (TPR) domain of KLC. The N-terminal capping helix of the TPR domain exhibits an atypical sequence and structural features that may contribute to the versatility of the TPR domain to bind different cargos. We determined crystal structures of the TPR domain of both KLC1 and KLC2 encompassing the N-terminal capping helix and show that this helix exhibits two distinct and defined orientations relative to the rest of the TPR domain. Such a difference in orientation gives rise, at the N-terminal part of the groove, to the formation of one hydrophobic pocket, as well as to electrostatic variations at the groove surface. We present a comprehensive structural analysis of available KLC1/2-TPR domain structures that highlights that ligand binding into the groove can be specific of one or the other N-terminal capping helix orientations. Further, structural analysis reveals that the N-terminal capping helix is always involved in crystal packing contacts, especially in a TPR1:TPR1' contact which highlights its propensity to be a protein-protein interaction site. Together, these results underline that the structural plasticity of the N-terminal capping helix might represent a structural determinant for TPR domain structural versatility in cargo binding. | |||
Structural plasticity of the N-terminal capping helix of the TPR domain of kinesin light chain.,Nguyen TQ, Chenon M, Vilela F, Velours C, Aumont-Nicaise M, Andreani J, Varela PF, Llinas P, Menetrey J PLoS One. 2017 Oct 16;12(10):e0186354. doi: 10.1371/journal.pone.0186354., eCollection 2017. PMID:29036226<ref>PMID:29036226</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5ojf" style="background-color:#fffaf0;"></div> | ||
[[Category: Andreani | |||
[[Category: Fernandez-Varela | ==See Also== | ||
[[Category: | *[[Kinesin 3D Structures|Kinesin 3D Structures]] | ||
[[Category: | == References == | ||
[[Category: Nguyen | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Andreani J]] | |||
[[Category: Chenon M]] | |||
[[Category: Fernandez-Varela P]] | |||
[[Category: Llinas P]] | |||
[[Category: Menetrey J]] | |||
[[Category: Nguyen TQ]] | |||
[[Category: Velours C]] | |||
[[Category: Vilela F]] | |||
Latest revision as of 19:51, 13 December 2023
Crystal Structure of KLC2-TPR domain (fragment [A1-B6]Crystal Structure of KLC2-TPR domain (fragment [A1-B6]
Structural highlights
FunctionPublication Abstract from PubMedKinesin1 plays a major role in neuronal transport by recruiting many different cargos through its kinesin light chain (KLC). Various structurally unrelated cargos interact with the conserved tetratricopeptide repeat (TPR) domain of KLC. The N-terminal capping helix of the TPR domain exhibits an atypical sequence and structural features that may contribute to the versatility of the TPR domain to bind different cargos. We determined crystal structures of the TPR domain of both KLC1 and KLC2 encompassing the N-terminal capping helix and show that this helix exhibits two distinct and defined orientations relative to the rest of the TPR domain. Such a difference in orientation gives rise, at the N-terminal part of the groove, to the formation of one hydrophobic pocket, as well as to electrostatic variations at the groove surface. We present a comprehensive structural analysis of available KLC1/2-TPR domain structures that highlights that ligand binding into the groove can be specific of one or the other N-terminal capping helix orientations. Further, structural analysis reveals that the N-terminal capping helix is always involved in crystal packing contacts, especially in a TPR1:TPR1' contact which highlights its propensity to be a protein-protein interaction site. Together, these results underline that the structural plasticity of the N-terminal capping helix might represent a structural determinant for TPR domain structural versatility in cargo binding. Structural plasticity of the N-terminal capping helix of the TPR domain of kinesin light chain.,Nguyen TQ, Chenon M, Vilela F, Velours C, Aumont-Nicaise M, Andreani J, Varela PF, Llinas P, Menetrey J PLoS One. 2017 Oct 16;12(10):e0186354. doi: 10.1371/journal.pone.0186354., eCollection 2017. PMID:29036226[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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