Mapping functional interaction sites of human prune C-terminal domain by NMR spectroscopy in human cell lysates.
Get well prune: The C-terminal third domain of h-prune is largely unfolded and involved in relevant protein-protein interactions, particularly with Nm23-H1 (see figure), GSK-3β and gelsolin. This study shows that protein functions mediated by protein-protein interactions can be accurately followed in cell lysates by using fast NMR spectroscopy, which could be easily used for a very efficient NMR drug-discovery strategy.
Istituto di Biostrutture e Bioimmagini, CNR via Mezzocannone 16, 80134, Napoli (Italy).
Donatella
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Diana
Giovanni
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Smaldone
Pasquale
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De Antonellis
Luciano
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Pirone
MariaNeve
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Carotenuto
Alessandro
A
Alonzi
Sonia
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Di Gaetano
Massimo
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Zollo
Emilia M
EM
Pedone
Roberto
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Fattorusso
D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D003585:Cell Biology; D055808:Drug Discovery; D018260:Gelsolin / Q000737:chemistry; D038362:Glycogen Synthase Kinase 3 / Q000737:chemistry* / Q000378:metabolism; D000071679:Glycogen Synthase Kinase 3 beta; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D054778:NM23 Nucleoside Diphosphate Kinases / Q000737:chemistry* / Q000378:metabolism; D010744:Phosphoric Monoester Hydrolases
D002352:Carrier Proteins; D018260:Gelsolin; D054778:NM23 Nucleoside Diphosphate Kinases; C000605506:GSK3B protein, human; D000071679:Glycogen Synthase Kinase 3 beta; D038362:Glycogen Synthase Kinase 3; C438732:PRUNE1 protein, human; D010744:Phosphoric Monoester Hydrolases
NMR spectroscopy; human cell lysates; intrinsically disordered proteins; protein-protein interactions; structure elucidation