SPring-8, the large synchrotron radiation facility

Skip to content
Personal tools

Elucidation of Mechanism of Sulfation Reaction of the Protein Tyrosine Holding the Key to Viral Invasion (Press Release)

Release Date
13 Mar, 2013
  • BL38B1 (Structural Biology III)
- Expectation for development of new pharmaceuticals -

Kyushu University
University of Miyazaki

The crystal structure of human tyrosylprotein sulfotransferase was determined in the form of a complex with a target protein, and the mechanism of its action was elucidated for the first time in the world by a joint research group including Yoshimitsu Kakuta (associate professor) from the Graduate School of the Faculty of Agriculture, Kyushu University, and Masahito Suiko (professor) and Yoichi Sakakibara (professor) from the Faculty of Agriculture, the University of Miyazaki. This sulfotransferase acts to attach a marker (sulfate group) to various types of protein. The sulfate group attached to the protein is not only related to various types of biological defense mechanism but also used in viral invasion into a human cell. The elucidated sulfate-group attachment mechanism is expected to contribute to the development of new medicines including antiviral agents.

The results of this research were published in Nature Communications, an offshoot of the international scientific journal Nature, on 12 March 2013.

"Crystal structure of human tyrosylprotein sulfotransferase-2 reveals the mechanism of protein tyrosine sulfation reaction"
Takamasa Teramoto, Yukari Fujikawa, Yoshirou Kawaguchi, Katsuhisa Kurogi, Masayuki Soejima, Rumi Adachi, Yuichi Nakanishi, Emi Mishiro-Sato, Ming-Cheh Liu, Yoichi Sakakibara, Masahito Suiko, Makoto Kimura, and Yoshimitsu Kakuta
Nature Communications 4, Published 12 March 2013


Fig. 1	Modification by sulfation
Fig. 1 Modification by sulfation

Fig. 2	Modification by sulfation serves as a marker at the time of viral infection
Fig. 2 Modification by sulfation serves as a marker at the time of viral infection

Fig. 3
Fig. 3

*1 Tyrosine residue

A side chain of tyrosine, one of the amino acids constituting proteins. It is characterized by a phenolic hydroxyl group.

*2 Dimer
A molecule consisting of two identical simpler molecules (particularly polymers) bound together.

For more information, please contact:
  Associate Prof. Yoshimitsu Kakuta (Kyushu University)
    E-mail : mail1

  Prof. Masahito Suiko (University of Miyazaki)
    E-mail : mail1

  Prof. Yoichi Sakakibara (University of Miyazaki)
    E-mail : mail1