6pq2
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Structural Basis for Client Recognition and Activity of Hsp40 Chaperones== | |
- | + | <StructureSection load='6pq2' size='340' side='right'caption='[[6pq2]]' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[6pq2]] 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=6PQ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PQ2 FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=6pq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pq2 OCA], [https://pdbe.org/6pq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pq2 RCSB], [https://www.ebi.ac.uk/pdbsum/6pq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pq2 ProSAT]</span></td></tr> |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/PPB_ECOLI PPB_ECOLI] [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> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Thermus thermophilus]] | ||
+ | [[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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