9dyv: Difference between revisions
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==Assembly and functional mechanisms of the Hsp70-Hsp40 chaperone machinery== | |||
<StructureSection load='9dyv' size='340' side='right'caption='[[9dyv]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9dyv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9DYV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9DYV FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> | |||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9dyv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9dyv OCA], [https://pdbe.org/9dyv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9dyv RCSB], [https://www.ebi.ac.uk/pdbsum/9dyv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9dyv ProSAT]</span></td></tr> | ||
[[Category: Ibrahim | </table> | ||
[[Category: Jiang | == Function == | ||
[[Category: | [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> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermus thermophilus]] | |||
[[Category: Ibrahim Z]] | |||
[[Category: Jiang Y]] | |||
[[Category: Kalodimos CG]] | |||
[[Category: Xia Y]] | |||
Latest revision as of 09:06, 22 October 2025
Assembly and functional mechanisms of the Hsp70-Hsp40 chaperone machinery
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