6gjh: Difference between revisions

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 <StructureSection load='6gjh' size='340' side='right'caption='[[6gjh]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6gjh]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GJH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GJH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6gjh]] is a 12 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=6GJH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GJH FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSPB1, HSP27, HSP28 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6gjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gjh OCA], [http://pdbe.org/6gjh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gjh RCSB], [http://www.ebi.ac.uk/pdbsum/6gjh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gjh ProSAT]</span></td></tr>
 </table>
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 == Function ==
 [[http://www.uniprot.org/uniprot/HSPB1_HUMAN HSPB1_HUMAN]] Involved in stress resistance and actin organization.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Mechanical force-induced conformational changes in proteins underpin a variety of physiological functions, typified in muscle contractile machinery. Mutations in the actin-binding protein filamin C (FLNC) are linked to musculoskeletal pathologies characterized by altered biomechanical properties and sometimes aggregates. HspB1, an abundant molecular chaperone, is prevalent in striated muscle where it is phosphorylated in response to cues including mechanical stress. We report the interaction and up-regulation of both proteins in three mouse models of biomechanical stress, with HspB1 being phosphorylated and FLNC being localized to load-bearing sites. We show how phosphorylation leads to increased exposure of the residues surrounding the HspB1 phosphosite, facilitating their binding to a compact multidomain region of FLNC proposed to have mechanosensing functions. Steered unfolding of FLNC reveals that its extension trajectory is modulated by the phosphorylated region of HspB1. This may represent a posttranslationally regulated chaperone-client protection mechanism targeting over-extension during mechanical stress.
+HspB1 phosphorylation regulates its intramolecular dynamics and mechanosensitive molecular chaperone interaction with filamin C.,Collier MP, Alderson TR, de Villiers CP, Nicholls D, Gastall HY, Allison TM, Degiacomi MT, Jiang H, Mlynek G, Furst DO, van der Ven PFM, Djinovic-Carugo K, Baldwin AJ, Watkins H, Gehmlich K, Benesch JLP Sci Adv. 2019 May 22;5(5):eaav8421. doi: 10.1126/sciadv.aav8421. eCollection 2019, May. PMID:31131323<ref>PMID:31131323</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 6gjh" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
+[[Category: Human]]
 [[Category: Large Structures]]
 [[Category: Benesch, J L.P]]