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==Structural Basis for Client Recognition and Activity of Hsp40 Chaperones==
<StructureSection load='6pri' size='340' side='right'caption='[[6pri]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6pri]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] 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=6PRI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PRI 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=6pri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pri OCA], [https://pdbe.org/6pri PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pri RCSB], [https://www.ebi.ac.uk/pdbsum/6pri PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pri 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/PPB_ECOLI PPB_ECOLI] 
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6pri" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Thermus thermophilus HB8]]
[[Category: Jiang Y]]
[[Category: Kalodimos CG]]
[[Category: Rossi P]]