Mikako Shirouzu
National Institute of Advanced Industrial Science and Technology
Network
Latest external collaboration on country level. Dive into details by clicking on the dots.
Publication
Featured researches published by Mikako Shirouzu.
Journal of Biological Chemistry | 2005
Naoki Takada; Mariko Hatakeyama; Mio Ichikawa; Xiaomei Yu; Kentaro Tomii; Noriaki Okimoto; Noriyuki Futatsugi; Tetsu Narumi; Mikako Shirouzu; Shigeyuki Yokoyama; Akihiko Konagaya; Makoto Taiji
Ligand-activated and tyrosine-phosphorylated ErbB3 receptor binds to the SH2 domain of the p85 subunit of phosphatidylinositol 3-kinase and initiates intracellular signaling. Here, we studied the interactions between the N- (N-SH2) and C- (C-SH2) terminal SH2 domains of the p85 subunit of the phosphatidylinositol 3-kinase and eight ErbB3 receptor-derived phosphotyrosyl peptides (P-peptides) by using molecular dynamics, free energy, and surface plasmon resonance (SPR) analyses. In SPR analysis, these P-peptides showed no binding to the C-SH2 domain, but P-peptides containing a phospho-YXXM or a non-phospho-YXXM motif did bind to the N-SH2 domain. The N-SH2 domain has two phosphotyrosine binding sites in its N- (N1) and C- (N2) terminal regions. Interestingly, we found that P-peptides of pY1180 and pY1241 favored to bind to the N2 site, although all other P-peptides showed favorable binding to the N1 site. Remarkably, two phosphotyrosines, pY1178 and pY1243, which are just 63 amino acids apart from the pY1241 and pY1180, respectively, showed favorable binding to the N1 site. These findings indicate a possibility that the pair of phosphotyrosines, pY1178-pY1241 or pY1243-pY1180, will fold into an appropriate configuration for binding to the N1 and N2 sites simultaneously. Our model structures of the cytoplasmic C-terminal domain of ErbB3 receptor also strongly supported the speculation. The calculated binding free energies between the N-SH2 domain and P-peptides showed excellent qualitative agreement with SPR data with a correlation coefficient of 0.91. The total electrostatic solvation energy between the N-SH2 domain and P-peptide was the dominant factor for its binding affinity.
Biochemistry | 2003
Mariko Hatakeyama; Mio Ichikawa; Xiaomei Yu; Noriyuki Futatsugi; Tetsu Narumi; Kazuhiko Fukui; Takaho Terada; Makoto Taiji; Mikako Shirouzu; Shigeyuki Yokoyama; Akihiko Konagaya
Archive | 2002
Shigeyuki Yokoyama; Hideo Ogiso; Mikako Shirouzu; Osamu Nureki; Ryuichiro Ishitani; Kazuki Saito; Tomokazu Matsusue; Naoki Nakao; Hiroyuki Muramatsu; Mikihiko Shinozaki
Archive | 2002
Kaori Tajima; Takanori Kigawa; Mikako Shirouzu; Takashi Yabuki; Goushi Ishihara; Shigeyuki Yokoyama
Archive | 2003
Mikako Shirouzu; Alexander A. Tokmakov; Shigeyuki Yokoyama
Archive | 2003
Mikako Shirouzu; Goushi Ishihara; Mihoro Saeki; Mie Goto; Kaori Tajima; Takanori Kigawa; Shigeyuki Yokoyama
Archive | 2004
Mikako Shirouzu; Goushi Ishihara; Mihoro Saeki; Mie Goto; Kaori Tajima; Takanori Kigawa; Shigeyuki Yokoyama
Archive | 2004
Natsuko Matsuda; Takanori Kigawa; Namtip Chumpolkulwong; Chie Takemoto; Mikako Shirouzu; Akiko Tanaka; Shigeyuki Yokoyama
Archive | 2003
Shigeyuki Yokoyama; Mikako Shirouzu; Ayako Sakamoto; Kensaku Sakamoto
Archive | 2008
Shigeyuki Yokoyama; Kazumi Shimono; Mikako Shirouzu; Mie Goto
Collaboration
Dive into the Mikako Shirouzu's collaboration.
National Institute of Advanced Industrial Science and Technology
View shared research outputs