Mapping functional interaction sites of human prune C-terminal domain by NMR spectroscopy in human cell lysates

Chemistry. 2013 Sep 9;19(37):12217-20. doi: 10.1002/chem.201302168. Epub 2013 Aug 12.

Abstract

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.

Keywords: NMR spectroscopy; human cell lysates; intrinsically disordered proteins; protein-protein interactions; structure elucidation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carrier Proteins / chemistry*
  • Carrier Proteins / metabolism
  • Cell Biology
  • Drug Discovery
  • Gelsolin / chemistry
  • Glycogen Synthase Kinase 3 / chemistry*
  • Glycogen Synthase Kinase 3 / metabolism
  • Glycogen Synthase Kinase 3 beta
  • Humans
  • Magnetic Resonance Spectroscopy
  • NM23 Nucleoside Diphosphate Kinases / chemistry*
  • NM23 Nucleoside Diphosphate Kinases / metabolism
  • Phosphoric Monoester Hydrolases

Substances

  • Carrier Proteins
  • Gelsolin
  • NM23 Nucleoside Diphosphate Kinases
  • GSK3B protein, human
  • Glycogen Synthase Kinase 3 beta
  • Glycogen Synthase Kinase 3
  • PRUNE1 protein, human
  • Phosphoric Monoester Hydrolases