4.6 Article

Biophysical characterization of Ca2+-binding of S100A5 and Ca2+-induced interaction with RAGE

期刊

出版社

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2016.12.143

关键词

Ca2+ binding; Calorimetry; NMR spectroscopy; RAGE; S100A5

资金

  1. National Research Foundation of Korea [2013R1A1A2010856]
  2. Cooperative Research Program for Agriculture Science & Technology Development, Rural Development Administration [PJ011112016]
  3. Korea Basic Science Institute grant [T36412]
  4. New & Renewable Energy Core Technology Program of the Korea Institute of Energy Technology Evaluation and Planning from the Ministry of Trade, Industry & Energy, Republic of Korea [20143030090940]
  5. National Research Foundation of Korea [2013R1A1A2010856] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
  6. Rural Development Administration (RDA), Republic of Korea [PJ011112022017] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)

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S100A5 is a calcium-binding protein of S100 family, which represents a major ligand to the receptor for advanced glycation end product (RAGE), a pattern recognition receptor engaged in diverse pathological processes. Here we have characterized calcium binding of S100A5 and the complex formation between S100A5 and RAGE using calorimetry and NMR spectroscopy. S100A5 binds to calcium ions in a sequential manner with the equilibrium dissociation constants (K-D) of 1.3 mu M and 3.5 mu M, which corresponds to the calcium-binding at the C-terminal and N-terminal EF-hands. Upon calcium binding, S100A5 interacts with the V domain of RAGE (RAGE-v) to form a heterotrimer (K-D similar to 5.9 mu M) that is distinct among the S100 family proteins. Chemical shift perturbation data from NMR titration experiments indicates that S100A5 employs the periphery of the dimer interface to interact with RAGE-v. Distinct binding mode and stoichiometry of RAGE against different S100 family proteins could be important to modulate diverse RAGE signaling. (C) 2016 Elsevier Inc. All rights reserved.

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