Title : Conformational changes at the nucleotide binding of GroEL induced by binding of protein substrates. Luminescence studies.

Pub. Date : 1997 Aug 8

PMID : 9242617






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 2"-Deoxy-3"-anthraniloyl adenosine-5-triphosphate (ANT-dATP) coordinated to Tb3+ was used as an environmentally sensitive probe of the nucleotide-binding site of GroEL. tb3+ heat shock protein family D (Hsp60) member 1 Homo sapiens
2 Tb3+.ANT-dATP recognizes the nucleotide-binding site of GroEL and inhibits ATPase activity. tb3+ heat shock protein family D (Hsp60) member 1 Homo sapiens
3 Sensitized luminescence, arising from resonance energy transfer from the anthraniloyl moiety to Tb3+, is substantially enhanced in the presence of GroEL. tb3+ heat shock protein family D (Hsp60) member 1 Homo sapiens
4 Binding of denatured mitochondrial malate dehydrogenase to the apical domain of GroEL causes a red shift in the fluorescence emitted by anthraniloyl and further enhancement in the phosphorescence emitted by Tb3+ upon excitation at 320 nm. tb3+ heat shock protein family D (Hsp60) member 1 Homo sapiens