6fv0: Difference between revisions
m Protected "6fv0" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of the TPR domain of KLC1 in complex with the C-terminal peptide of torsinA== | |||
<StructureSection load='6fv0' size='340' side='right' caption='[[6fv0]], [[Resolution|resolution]] 2.29Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6fv0]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FV0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FV0 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6fv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fv0 OCA], [http://pdbe.org/6fv0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fv0 RCSB], [http://www.ebi.ac.uk/pdbsum/6fv0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fv0 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Kinesin-mediated cargo transport is required for many cellular functions and plays a key role in pathological processes. Structural information on how kinesins recognize their cargoes is required for a molecular understanding of this fundamental and ubiquitous process. Here, we present the crystal structure of the tetratricopeptide repeat of kinesin light chain 2 in complex with a cargo peptide harboring a 'tryptophan-acidic' motif derived from SKIP, a critical host determinant in Salmonella pathogenesis and a regulator of lysosomal positioning. Structural data together with biophysical, biochemical, and cellular assays allow us to propose a framework for intracellular transport based on the binding by kinesin-1 of W-acidic cargo motifs through a combination of electrostatic interactions and sequence-specific elements, providing direct molecular evidence of the mechanisms for kinesin-1:cargo recognition. | |||
Structural Basis For Kinesin-1:Cargo Recognition.,Pernigo S, Lamprecht A, Steiner RA, Dodding MP Science. 2013 Mar 21. PMID:23519214<ref>PMID:23519214</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 6fv0" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Dodding, M P]] | |||
[[Category: Pernigo, S]] | [[Category: Pernigo, S]] | ||
[[Category: Steiner, R A]] | |||
[[Category: Cargo recognition]] | |||
[[Category: Motor protein]] | |||
[[Category: Nanobody]] | |||
[[Category: Protein complex]] | |||
Revision as of 09:43, 28 March 2018
Crystal structure of the TPR domain of KLC1 in complex with the C-terminal peptide of torsinACrystal structure of the TPR domain of KLC1 in complex with the C-terminal peptide of torsinA
Structural highlights
Publication Abstract from PubMedKinesin-mediated cargo transport is required for many cellular functions and plays a key role in pathological processes. Structural information on how kinesins recognize their cargoes is required for a molecular understanding of this fundamental and ubiquitous process. Here, we present the crystal structure of the tetratricopeptide repeat of kinesin light chain 2 in complex with a cargo peptide harboring a 'tryptophan-acidic' motif derived from SKIP, a critical host determinant in Salmonella pathogenesis and a regulator of lysosomal positioning. Structural data together with biophysical, biochemical, and cellular assays allow us to propose a framework for intracellular transport based on the binding by kinesin-1 of W-acidic cargo motifs through a combination of electrostatic interactions and sequence-specific elements, providing direct molecular evidence of the mechanisms for kinesin-1:cargo recognition. Structural Basis For Kinesin-1:Cargo Recognition.,Pernigo S, Lamprecht A, Steiner RA, Dodding MP Science. 2013 Mar 21. PMID:23519214[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||