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Nm23-H1/NDP kinase folding intermediates and cancer: a hypothesis.

Abstract
The Nm23-H1/nucleoside diphosphate (NDP) kinase A is a metastasis suppressor, besides its enzymatic activity. The mutant S120G has been found in high-grade neuroblastomas. The mutant protein, once denatured in urea, is unable to refold in vitro. A size-exclusion chromatography analysis of the folding/association pathway showed that recombinant wild-type and S120G mutant human Nm23-H1/NDP kinase A unfold and refold passing through a molten globule state while typical hexameric NDP kinases unfold without dissociated species and refold through a native monomeric intermediate. A survey of the recent literature showed that several proteins involved in cancer, and their mutants, are marginally stable, like the wild-type Nm23-H1/NDP kinase A, or are misfolded, like its S120G mutant. We therefore suggest that the low thermodynamic stability and the folding intermediate of the Nm23-H1/NDP kinase A may be necessary for its regulatory properties.
AuthorsIoan Lascu
JournalJournal of bioenergetics and biomembranes (J Bioenerg Biomembr) Vol. 38 Issue 3-4 Pg. 265-8 (Aug 2006) ISSN: 0145-479X [Print] United States
PMID16944300 (Publication Type: Journal Article)
Chemical References
  • NM23 Nucleoside Diphosphate Kinases
  • Tumor Suppressor Proteins
  • NME1 protein, human
  • Nucleoside-Diphosphate Kinase
Topics
  • Chromatography, Gel
  • Humans
  • Mutation, Missense (genetics)
  • NM23 Nucleoside Diphosphate Kinases
  • Neuroblastoma (genetics)
  • Nucleoside-Diphosphate Kinase (genetics)
  • Protein Folding
  • Thermodynamics
  • Tumor Suppressor Proteins (genetics)

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