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| | <StructureSection load='5lum' size='340' side='right'caption='[[5lum]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='5lum' size='340' side='right'caption='[[5lum]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5lum]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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://proteopedia.org/fgij/fg.htm?mol=5LUM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5lum]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5LUM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSPB6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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://proteopedia.org/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> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5lum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lum OCA], [https://pdbe.org/5lum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lum RCSB], [https://www.ebi.ac.uk/pdbsum/5lum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lum ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/HSPB6_HUMAN HSPB6_HUMAN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Antson, A A]] | + | [[Category: Antson AA]] |
| - | [[Category: Beelen, S]] | + | [[Category: Beelen S]] |
| - | [[Category: Gusev, N B]] | + | [[Category: Gusev NB]] |
| - | [[Category: Kulikova, A A]] | + | [[Category: Kulikova AA]] |
| - | [[Category: Sluchanko, N N]] | + | [[Category: Sluchanko NN]] |
| - | [[Category: Strelkov, S V]] | + | [[Category: Strelkov SV]] |
| - | [[Category: Weeks, S D]] | + | [[Category: Weeks SD]] |
| - | [[Category: Chaperone protein]]
| + | |
| - | [[Category: Idr]]
| + | |
| - | [[Category: Protein-peptide complex]]
| + | |
| Structural highlights
Function
HSPB6_HUMAN
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sluchanko NN, Beelen S, Kulikova AA, Weeks SD, Antson AA, Gusev NB, Strelkov SV. Structural Basis for the Interaction of a Human Small Heat Shock Protein with the 14-3-3 Universal Signaling Regulator. Structure. 2016 Dec 30. pii: S0969-2126(16)30395-1. doi:, 10.1016/j.str.2016.12.005. PMID:28089448 doi:http://dx.doi.org/10.1016/j.str.2016.12.005
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