ニュース

「Biophysics and Physicobiology」にYuhi Hosoe et al. “Structural and functional properties of Grb2 SH2 dimer in CD28 binding”を掲載

2019年02月22日 学会から

日本生物物理学会欧文誌[Biophysics and Physicobiology]に以下の論文が新規掲載されました。

Yuhi Hosoe, Nobutaka Numoto, Satomi Inaba, Shuhei Ogawa, Hisayuki Morii, Ryo Abe, Nobutoshi Ito and Masayuki Oda “Structural and functional properties of Grb2 SH2 dimer in CD28 binding”

【Significance】
Folding and CD28 binding properties of Grb2 SH2 dimer

We purified the stable form of Grb2 SH2 dimer and monomer, and analyzed their structural and functional properties. The dimer mostly dissociated into the monomer around 50ºC. The CD28 binding affinity of dimer was about three fold higher than that of monomer. The stable dimer would be swapped dimer, in which the C-terminal region is extended towards the adjacent molecule. Because Trp121 was considered to be the key residue for dimer formation, W121S mutant was generated and its structural and functional properties were analyzed. The mutant still formed dimers, but lost the ability to bind CD28.


Biophysics and Physicobiology, Vol.16, pp. 80-88
URL: https://doi.org/10.2142/biophysico.16.0_80


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