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RISS 인기검색어
- 검색키워드
- 저자 : Katsutoshi Nitta (검색결과 2 건)
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Structure and Activity of Insect Cytokine GBP which Stimulates the EGF Receptor
Tomoyasu Aizawa,Yoichi Hayakawa,Katsutoshi Nitta,Keiichi Kawano 한국분자세포생물학회 2002 Molecules and cells Vol.14 No.1
Growth-blocking peptide (GBP) is an insect cytokine that possesses diverse biological activities such as lar-val growth regulation, cell proliferation, and stimula-tion of immune cells. GBP is a 25-amino acid peptide with one disulfide bond. It has been revealed that the tertiary structure of GBP consists of an N- and C- terminal disordered region and a well-structured core. Although there is only a slight similarity between the primary structures of GBP and EGF and the molecu-lar weight of GBP is about half that of EGF, GBP di-rectly binds and activates the EGF receptor of human keratinocyte cells. Furthermore, the tertiary structure of the well-defined region of GBP is similar to that of the C-terminal domain of EGF. This review will focus on the tertiary structure of GBP and its activities, as compared with those of EGF.
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The Effect of S130A Mutant of pharaonis Halorhodopsin on Ability of Chloride Binding and Photocycle
Sato, Maki,Kikukawa, Takashi,Araiso, Tsunehisa,Okita, Hirotaka,Shimono, Kazumi,Kamo, Naoki,Demura, Makoto,Nitta, Katsutoshi Korean Society of Photoscience 2002 Journal of Photosciences Vol.9 No.2
Bacteriorhodopsin (bR) and halorhodopsin (hR), which exist in the membrane of Halobacterium salinarum, are light-driven ion pumps. In spite of high similarity of primary and tertiary structures between bR and hR, these membrane proteins transport different ions, proton and chloride, in the opposite direction. From alignment of the amino acid sequences, Thr-89 of bR is homologous to Ser-l15 of hR from Halobacterium salinarum (shR). X-ray structure of shR has revealed that OH group of this residue directly interacts with CI$\^$-/ Thus, Ser-lI5 of shR is expected to play an important role in CI$\^$-/ binding and transport. In this study, we expressed wild type hR from Natronobacterium pharaonis (PhR) and Sl30A, which corresponds to Ser-l15 of shR, in E. coli in order to clarify binding affinity of chloride ion and photocycle reactions. From the titration with CI$\^$-/, affinity of Sl30A became quite lower than that of WT (WT 6 mM, Sl30A 89 mM). Furthermore, from the flash photolysis with pulse laser of λ$\_$max/ at 532 nm, the reaction rate of SI30A from 0 intermediate to hR ground state was found to become apparently slower than that of WT. The singular value decomposition (SVD) and global fitting analyses of the photocycles were performed to identify all photointermediates and determine the reaction rates.
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