Structural biological studies on the sialic acid-binding mechanism of R-type lectin mutant

2014 Fiscal Year Final Research Report

• Project/Area Number: 24580500
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Applied molecular and cellular biology
• Research Institution: National Agriculture and Food Research Organization
• Principal Investigator: HEMMI Hikaru 独立行政法人農業・食品産業技術総合研究機構, 食品総合研究所食品分析研究領域, 上席研究員 (70353993)
• Co-Investigator(Kenkyū-buntansha): KUNO Atsushi 独立行政法人産業技術総合研究所, 糖鎖創薬技術研究センター, 上級主任研究員 (50302287) ; HIRABAYASHI Jun 独立行政法人産業技術総合研究所, 幹細胞工学研究センター, 首席研究員 (40156691)
• Project Period (FY): 2012-04-01 – 2015-03-31
• Keywords: 蛋白質 / 糖鎖 / NMR / レクチン / 糖認識ドメイン

Outline of Final Research Achievements

We performed the nuclear magnetic resonance analysis of the sialic acid-binding mechanism of the novel sialic acid-binding lectin (SRC) produced from the C-terminal domain of the novel R-type lectin from the earthworm (EW29Ch) by natural evolution-mimicry. The results showed that in the 6’-sialyllactose-bound state SRC has two conformations different from both the conformation in the sugar-free state and that in the lactose-bound state. Further, the internal motion of the loop region in subdomain γ of SRC remarkably changed from that of the corresponding region in subdomain γ of the wild type lectin EW29Ch, indicating that the internal motion change is important in the sialic acid-binding mechanism of SRC.

Free Research Field

構造生物学