Random coil conformation of a Gly/Ala-rich insert in IκBα excludes structural stabilization as the mechanism for protection against proteasomal degradation

Ainars Leonchiks, Edvards Liepinsh, Mikhail Barishev, Anatoly Sharipo, Maria G. Masucci, Gottfried Otting

Research output: Contribution to journalArticlepeer-review

16 Citations (Scopus)

Abstract

Peptide segments of multiple glycine and alanine residues prevent the proteolytic degradation of ubiquitinated proteins by the proteasome. The structure of a Gly/Ala-rich insert in IκBα was probed by nuclear magnetic resonance (NMR) spectroscopy, comparing IκBα samples with and without Gly/Ala-rich insert. Narrow 1H-NMR resonances at chemical shifts indicative of random coil conformations were observed in the difference spectrum. circular dichroism (CD) measurements further confirm that the mechanism of protection against proteolytic degradation is not based on structural transition or stabilization caused by the Gly/Ala-rich segment. In addition, most of the N- and C-terminal residues outside the ankyrin repeats in wild-type IκBα were found to be flexibly disordered. Copyright (C) 1998 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)365-369
Number of pages5
JournalFEBS Letters
Volume440
Issue number3
DOIs
Publication statusPublished - 4 Dec 1998

Keywords

  • Amino acid analysis
  • Gly/Ala-rich peptide
  • IκBα
  • Nuclear magnetic resonance
  • Random coil conformation

Field of Science

  • 1.6 Biological sciences

Publication Type

  • 1.1. Scientific article indexed in Web of Science and/or Scopus database

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