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

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• 作者：Iktae Kim^a ; ^{iktaekim@snu.ac.kr} ; Ko On Lee^a ; ^{koonlee@snu.ac.kr} ; Young-Joo Yun^a ; Jea Yeon Jeong^a ; Eun-Hee Kim^b ; Haekap Cheong^b ; Kyoung-Seok Ryu^b ; Nak-Kyoon Kim^c ; Jeong-Yong Suh^a ; ^{jysuh@snu.ac.kr}
• 关键词：Ca2+ binding ; Calorimetry ; NMR spectroscopy ; RAGE ; S100A5
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2017
• 出版时间：29 January 2017
• 年：2017
• 卷：483
• 期：1
• 页码：332-338
• 全文大小：1132 K
• 卷排序：483

文摘

Thermodynamic of sequential Ca2+-binding to S100A5 is determined quantitatively. S100A5 binds to RAGE-v to form a distinct dynamic heterotrimer with KD ∼5.9 μM. RAGE-v binds to the rim of the S100A5 dimer interface via hydrophobic interaction. Different binding modes of S100 proteins to RAGE may modulate RAGE signaling.