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Ohara, Takashi; Umino, Hisao; Tamada, Taro; Kuroki, Ryota
no journal, ,
no abstracts in English
Arai, Shigeki; Tamada, Taro; Maeda, Yoshitake*; Kuroki, Ryota
no journal, ,
The mouse antibody TN1 recognizes the human thrombopoietin (hTPO) that primarily stimulates megakaryocytopoiesis and platelet production. In order to clarify the mechanism of the neutralizing activity of the TN1 antibody, the crystal structure of TN1-Fab was determined to 2.1 
resolution and was compared with that of TN1-Fab / hTPO complex (PDB id 1V7M and 1V7N). It was found that only side chain level "Induced-fit" upon the antigen binding was enough for TN1 to recognize hTPO. On the other hand, the relative angle of the variable- and constant-regions of the hTPO unbound form of TN1-Fab was slightly shifted from those of TN1-Fab / hTPO complex (rms deviation = 2.4 for all C
atoms of Fab). In this presentation, we will explain the details of the conformational change of the crystal structure of TN1-Fab fragment with and without binding of hTPO.
Ishida, Hisashi; Tsutsumi, Yu*; Matsumoto, Atsushi; Yura, Kei
no journal, ,
no abstracts in English
Adachi, Motoyasu; Honjo, Eijiro; Tamada, Taro; Blaber, M.*; Kuroki, Ryota
no journal, ,
Human acidic fibroblast growth factor (haFGF) is a powerful mitogen and angiogenic factor. Our objective is to reveal structure function relationships of haFGF by protein neutron crystallography. For the determination of neutron crystal structures, large crystal in size is required. Since haFGF forms thin crystals, we tried improvement of crystal growth by changing amino acids at molecular interface. The analysis using X-ray crystal structure showed that the residue of Glu81 is located near Glu81 generated by crystallographic symmetry. Therefore, Glu81 was replaced with Ala, Val, Leu, Ser and Thr residue. The mutants of E81S and E81T provided larger crystal in size than that of WT. The X-ray structures of E81S and E81T showed that a molecule of formic acid bridges between the two Glu81 residues by hydrogen bonding.
Tamada, Taro; Kinoshita, Takayoshi*; Tada, Toshiji*; Kurihara, Kazuo; Ohara, Takashi; Kuroki, Ryota
no journal, ,
no abstracts in English
Shoyama, Yoshinari; Tamada, Taro; Takeuchi, Ayako*; Taura, Futoshi*; Adachi, Motoyasu; Shoyama, Yukihiro*; Kuroki, Ryota; Morimoto, Satoshi*
no journal, ,
no abstracts in English
Kuroki, Ryota; Adachi, Motoyasu; Honjo, Eijiro; Kurihara, Kazuo; Ohara, Takashi; Tamada, Taro
no journal, ,
Determination of hydrogens by neutrons diffraction enables us to observe the ionization status of amino acids and the structural features of hydrogen bonds and hydrating waters. It is, however, needed to obtain a huge protein crystal because the intencity of neutron beam is weak in conparison with X-ray beam. Contribution of neutron crystallography has been limited because it needed more than 2mm
volume crystal and long term of data collection. Recent development on the palse sparation sourse is suposed to improve the efficiency of data collection more than 50 times, but necessity of a huge crystal still remains. In order to improve the size of the crystal, we have been working on the crystal lattice engineering to improve the volume of the crystal as well as the preparation of fully deuterated sample of proteins.
Kurihara, Kazuo; Tamada, Taro; Ohara, Takashi; Kuroki, Ryota
no journal, ,
no abstracts in English
Fujii, Satoshi*; Kono, Hidetoshi; Takenaka, Shigeori*; Go, Nobuhiro; Sarai, Akinori*
no journal, ,
no abstracts in English
Yonetani, Yoshiteru*; Fujii, Satoshi*; Sarai, Akinori*; Kono, Hidetoshi; Go, Nobuhiro
no journal, ,
no abstracts in English
Honjo, Eijiro; Tamada, Taro; Kuroki, Ryota
no journal, ,
no abstracts in English
Taguchi, Chiho*; Taura, Futoshi*; Morimoto, Satoshi*; Shoyama, Yoshinari; Tamada, Taro; Kuroki, Ryota; Shoyama, Yukihiro*
no journal, ,
no abstracts in English