Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

Dynamic nucleotide-dependent interactions of cysteine- and histidine-rich domain (CHORD)-containing Hsp90 cochaperones Chp-1 and melusin with cochaperones PP5 and Sgt1.

Hong TJ, Kim S, Wi AR, Lee P, Kang M, Jeong JH, Hahn JS

Mammals have two cysteine- and histidine-rich domain (CHORD)-containing Hsp90 cochaperones, Chp-1 and melusin, which are homologs of plant Rar1. It has been shown previously that Rar1 CHORD directly interacts with ADP bound to the nucleotide pocket of Hsp90. Here, we report that ADP and ATP can bind to Hsp90 cochaperones Chp-1 and PP5, inducing their conformational changes. Furthermore, we demonstrate ... [more]

J. Biol. Chem. Jan. 04, 2013; 288(1);215-22 [Pubmed: 23184943]

Throughput

  • Low Throughput

Additional Notes

  • figure 2.

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
CHORDC1 PPP5C
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
835871

Curated By

  • BioGRID