Title : Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, GRP94. II. Ligand-mediated activation of GRP94 molecular chaperone and peptide binding activity.

Pub. Date : 2000 Jul 28

PMID : 10816560






4 Functional Relationships(s)
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Protein Name
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1 Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, GRP94. adenosine nucleotide heat shock protein 90 beta family member 1 Homo sapiens
2 Although this domain is essential for Hsp90 function, the molecular basis for adenosine nucleotide-dependent regulation of GRP94, the endoplasmic reticulum paralog of Hsp90, remains to be established. adenosine nucleotide heat shock protein 90 beta family member 1 Homo sapiens
3 We report that bis-ANS (1,1"-bis(4-anilino-5-napthalenesulfonic acid), an environment sensitive fluorophore known to interact with nucleotide-binding domains, binds to the adenosine nucleotide-binding domain of GRP94 and thereby activates its molecular chaperone and peptide binding activities. adenosine nucleotide heat shock protein 90 beta family member 1 Homo sapiens
4 bis-ANS activation of GRP94 function was efficiently blocked by radicicol, an established inhibitory ligand for the adenosine nucleotide binding pocket. adenosine nucleotide heat shock protein 90 beta family member 1 Homo sapiens