Multilevel Changes in Protein Dynamics upon Complex Formation of the Calcium-Loaded S100A4 with a Nonmuscle Myosin IIA Tail Fragment

Gyula Pálfy, Bence Kiss, L. Nyitray, A. Bodor

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Dysregulation of Ca2+-binding S100 proteins plays important role in various diseases. The asymmetric complex of Ca2+-bound S100A4 with nonmuscle myosin IIA has high stability and highly increased Ca2+ affinity. Here we investigated the possible causes of this allosteric effect by NMR spectroscopy. Chemical shift-based secondary-structure analysis did not show substantial changes for the complex. Backbone dynamics revealed slow-timescale local motions in the H1 helices of homodimeric S100A4; these were less pronounced in the complex form and might be accompanied by an increase in dimer stability. Different mobilities in the Ca2+-coordinating EF-hand sites indicate that they communicate by an allosteric mechanism operating through changes in protein dynamics; this must be responsible for the elevated Ca2+ affinity. These multilevel changes in protein dynamics as conformational adaptation allow S100A4 fine-tuning of its protein–protein interactions inside the cell during Ca2+ signaling.

Original languageEnglish
Pages (from-to)1829-1838
Number of pages10
JournalChemBioChem
DOIs
Publication statusPublished - Oct 4 2016

Fingerprint

Nonmuscle Myosin Type IIA
Calcium
EF Hand Motifs
S100 Proteins
Cell Communication
Carrier Proteins
Proteins
Magnetic Resonance Spectroscopy
Chemical shift
Dimers
Nuclear magnetic resonance spectroscopy
Tuning

Keywords

  • backbone dynamics
  • Ca affinity
  • NMR spectroscopy
  • protein–protein interactions
  • S100A4 protein

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Organic Chemistry

Cite this

Multilevel Changes in Protein Dynamics upon Complex Formation of the Calcium-Loaded S100A4 with a Nonmuscle Myosin IIA Tail Fragment. / Pálfy, Gyula; Kiss, Bence; Nyitray, L.; Bodor, A.

In: ChemBioChem, 04.10.2016, p. 1829-1838.

Research output: Contribution to journalArticle

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