期刊
CHEMBIOCHEM
卷 17, 期 19, 页码 1829-1838出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201600280
关键词
backbone dynamics; Ca2+ affinity; NMR spectroscopy; protein-protein interactions; S100A4 protein
资金
- Hungarian National Research Fund (OTKA) [K108437, NK 101072]
- MedInProt
- EC [261863]
- European Union
- European Social Fund [TAMOP 4.2.1./B-09/KMR-2010-0003, TAMOP 4.2.4. A/1-11-1-2012-0001]
Dysregulation of Ca2+-binding S100 proteins plays important role in various diseases. The asymmetric complex of Ca2+-bound S100A4 with nonmuscle myosinIIA 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.
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