5lum: Difference between revisions

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'''Unreleased structure'''


The entry 5lum is ON HOLD  until Paper Publication
==Alpha-crystallin domain of human HSPB6 patched with its N-terminal peptide==
<StructureSection load='5lum' size='340' side='right' caption='[[5lum]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lum]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LUM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LUM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5lum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lum OCA], [http://pdbe.org/5lum PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lum RCSB], [http://www.ebi.ac.uk/pdbsum/5lum PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lum ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
By interacting with hundreds of protein partners, 14-3-3 proteins coordinate vital cellular processes. Phosphorylation of the small heat shock protein, HSPB6, within its intrinsically disordered N-terminal domain activates its interaction with 14-3-3, ultimately triggering smooth muscle relaxation. After analyzing the binding of an HSPB6-derived phosphopeptide to 14-3-3 using isothermal calorimetry and X-ray crystallography, we have determined the crystal structure of the complete assembly consisting of the 14-3-3 dimer and full-length HSPB6 dimer and further characterized this complex in solution using fluorescence spectroscopy, small-angle X-ray scattering, and limited proteolysis. We show that selected intrinsically disordered regions of HSPB6 are transformed into well-defined conformations upon the interaction, whereby an unexpectedly asymmetric structure is formed. This structure provides the first atomic resolution snapshot of a human small HSP in functional state, explains how 14-3-3 proteins sequester their regulatory partners, and can inform the design of small-molecule interaction modifiers to be used as myorelaxants.


Authors:  
Structural Basis for the Interaction of a Human Small Heat Shock Protein with the 14-3-3 Universal Signaling Regulator.,Sluchanko NN, Beelen S, Kulikova AA, Weeks SD, Antson AA, Gusev NB, Strelkov SV Structure. 2016 Dec 30. pii: S0969-2126(16)30395-1. doi:, 10.1016/j.str.2016.12.005. PMID:28089448<ref>PMID:28089448</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5lum" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Antson, A A]]
[[Category: Beelen, S]]
[[Category: Gusev, N B]]
[[Category: Kulikova, A A]]
[[Category: Sluchanko, N N]]
[[Category: Strelkov, S V]]
[[Category: Weeks, S D]]
[[Category: Chaperone protein]]
[[Category: Idr]]
[[Category: Protein-peptide complex]]
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