6prp
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structural Basis for Client Recognition and Activity of Hsp40 Chaperones== | |
| + | <StructureSection load='6prp' size='340' side='right'caption='[[6prp]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6prp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] and [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PRP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PRP FirstGlance]. <br> | ||
| + | </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=6prp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6prp OCA], [https://pdbe.org/6prp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6prp RCSB], [https://www.ebi.ac.uk/pdbsum/6prp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6prp ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DNAJ2_THET8 DNAJ2_THET8] Does not influence ATP binding or hydrolysis nor ADP release. Exerts influence on the interaction of DnaK with substrates; in the presence of DafA, DnaJ inhibits substrate binding, and substrate already bound to DnaK is displaced by DnaJ and DafA.<ref>PMID:10092456</ref> [https://www.uniprot.org/uniprot/DNAK_THET8 DNAK_THET8] Cooperates with DnaJ, GrpE and ClpB to reactivate heat-inactivated proteins.<ref>PMID:10377389</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Hsp70 and Hsp40 chaperones work synergistically in a wide range of biological processes including protein synthesis, membrane translocation, and folding. We used nuclear magnetic resonance spectroscopy to determine the solution structure and dynamic features of an Hsp40 in complex with an unfolded client protein. Atomic structures of the various binding sites in the client complexed to the binding domains of the Hsp40 reveal the recognition pattern. Hsp40 engages the client in a highly dynamic fashion using a multivalent binding mechanism that alters the folding properties of the client. Different Hsp40 family members have different numbers of client-binding sites with distinct sequence selectivity, providing additional mechanisms for activity regulation and function modification. Hsp70 binding to Hsp40 displaces the unfolded client. The activity of Hsp40 is altered in its complex with Hsp70, further regulating client binding and release. | ||
| - | + | Structural basis for client recognition and activity of Hsp40 chaperones.,Jiang Y, Rossi P, Kalodimos CG Science. 2019 Sep 20;365(6459):1313-1319. doi: 10.1126/science.aax1280. PMID:31604242<ref>PMID:31604242</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6prp" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermus thermophilus]] | ||
| + | [[Category: Thermus thermophilus HB8]] | ||
| + | [[Category: Jiang Y]] | ||
| + | [[Category: Kalodimos CG]] | ||
| + | [[Category: Rossi P]] | ||
Current revision
Structural Basis for Client Recognition and Activity of Hsp40 Chaperones
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