TY - JOUR
T1 - Interaction of S100A13 with C2 domain of receptor for advanced glycation end products (RAGE)
AU - Rani, Sandhya G.
AU - Sepuru, Krishna Mohan
AU - Yu, Chin
N1 - Funding Information:
We acknowledge financial support from the National Science Council (NSC) of Taiwan . We would like to thank the 700 MHz Nuclear Magnetic Resonance facility in the Chemistry Department, National Tsing Hua University.
Funding Information:
This research was supported by an operating grant from the National Science Council, Taiwan ( NSC 100-2113-M-007-012-MY3 ).
PY - 2014/9
Y1 - 2014/9
N2 - S100A13 is involved in several key biological functions like angiogenesis, tumor formation and cell apoptosis. It is a homodimeric protein that belongs to the S100 protein family. S100A13 is co-expressed with acidic fibroblast growth factor (FGF1) and interleukin-1α which are key angiogenesis inducers. The S100 proteins have been shown to be involved in several cellular functions such as calcium homeostasis, cell growth and differentiation dynamic of cytoskeleton. Its biological functions are mainly mediated through the receptor for advanced glycation end products (RAGE) signaling. RAGE is involved in inflammatory processes and is associated with diabetic complications, tumor outgrowth, and neurodegenerative disorders. RAGE induces cellular signaling upon binding of different ligands, such as S100 proteins, glycated proteins, and HMGB1. RAGE signaling is complex, and it depends on the cell type and concentration of the ligand. Molecular level interactions of RAGE and S100 proteins are useful to understand the RAGE signaling diversity. In this report we focus on the molecular level interactions of S100A13 and RAGE C2 domain. The binding between RAGE C2 and S100A13 is moderately strong (Kd ∼ 1.3 μM). We have solved the solution structure of the S100A13-RAGE C2 complex and pronounce the interface regions in S100A13-RAGE C2 complex which are helpful for drug development of RAGE induced diseases.
AB - S100A13 is involved in several key biological functions like angiogenesis, tumor formation and cell apoptosis. It is a homodimeric protein that belongs to the S100 protein family. S100A13 is co-expressed with acidic fibroblast growth factor (FGF1) and interleukin-1α which are key angiogenesis inducers. The S100 proteins have been shown to be involved in several cellular functions such as calcium homeostasis, cell growth and differentiation dynamic of cytoskeleton. Its biological functions are mainly mediated through the receptor for advanced glycation end products (RAGE) signaling. RAGE is involved in inflammatory processes and is associated with diabetic complications, tumor outgrowth, and neurodegenerative disorders. RAGE induces cellular signaling upon binding of different ligands, such as S100 proteins, glycated proteins, and HMGB1. RAGE signaling is complex, and it depends on the cell type and concentration of the ligand. Molecular level interactions of RAGE and S100 proteins are useful to understand the RAGE signaling diversity. In this report we focus on the molecular level interactions of S100A13 and RAGE C2 domain. The binding between RAGE C2 and S100A13 is moderately strong (Kd ∼ 1.3 μM). We have solved the solution structure of the S100A13-RAGE C2 complex and pronounce the interface regions in S100A13-RAGE C2 complex which are helpful for drug development of RAGE induced diseases.
KW - Isothermal titration calorimetry
KW - NMR spectroscopy
KW - RAGE dimerization
KW - Receptor for advanced glycation end products
KW - S100A13
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U2 - 10.1016/j.bbapap.2014.06.017
DO - 10.1016/j.bbapap.2014.06.017
M3 - Article
C2 - 24982031
AN - SCOPUS:84904582394
SN - 1570-9639
VL - 1844
SP - 1718
EP - 1728
JO - Biochimica et Biophysica Acta - Proteins and Proteomics
JF - Biochimica et Biophysica Acta - Proteins and Proteomics
IS - 9
ER -