Title : Adenosine nucleotides and the regulation of GRP94-client protein interactions.

Pub. Date : 2004 Jul 13

PMID : 15236592






3 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 We report that apo-GRP94 undergoes a time- and temperature-dependent tertiary conformational change that exposes a site(s) of protein-protein interaction; ATP, ADP, and radicicol markedly suppress this conformational change. Adenosine Diphosphate heat shock protein 90 beta family member 1 Homo sapiens
2 In concert with these findings, ATP and ADP act identically to suppress GRP94 homooligomerization, as well as both local and global conformational activity. Adenosine Diphosphate heat shock protein 90 beta family member 1 Homo sapiens
3 Whereas ATP elicited efficient release of BiP from both wild-type and mutant Ig heavy chain intermediates, GRP94 remained in stable association with Ig heavy chains in the presence of ATP or ADP. Adenosine Diphosphate heat shock protein 90 beta family member 1 Homo sapiens