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 - Basic Medicine (Core Departments) - Molecular Medicine
Cell Biology
Membrane proteins govern the basic cellular processes of signal transduction,the generation of electrical signals, molecular transport and energy conservation. In spite of the abundance and importance of membrane proteins there are only ca 120 unique membrane protein structures have been determined. Our laboratory is studying the structures of various membrane proteins and developing the methodologies in membrane protein crystallography in cooperation with ERATO Iwata Human Receptor Crystallography Project(, the MPL group at British synchrotron radiation facility, Diamond, and the MPC group( at Imperial College London. Our laboratory is ideal for the students aspired to build up an international career.

  So Iwata,Ph.D
Research and Education
The results of various genome projects have shown that up to 30% of human proteins occur in cell membranes. Membrane proteins play crucial roles in many biological functions and are of key importance for medicine. Over 50% of commercially available drugs target membrane proteins.

We are currently focusing to determine medically relevant membrane protein structures. These are the G protein-coupled receptors (GPCR), transporters (especially those for drugs, peptides, and sugars) and enzymes involved in steroid synthesis or metabolism. These membrane protein structures will provide a basic understanding of life at the molecular level and could boost computer aided rational design of new drugs, which could reduce the number of animal experiments and unwanted side effects.

Graduate students in our laboratory are expected to learn a series of techniques of protein crystallography from expression to X-ray crystallographic analysis and to solve a protein structure. The targets will be those listed above or related proteins. These projects are challenging but designed to be completed within a few years.

Cell Biology
Professor So Iwata

Takuya Kobayashi

Makoto Adachi,
Norimichi Nomura
TEL +81-75-753-4372
FAX +81-75-753-4660
Crystal structure of lactose permiase from Escherichia coli. A homologue of glucose transporters implicated in diabetes

Crystal structure of Photosystem II from  Thermosynechococcus elongates。Split water molecules using solar energy to evolve molecular oxygen in the atmosphere.
Recent Publications
1. Horsefield, R, Yankovskaya, V, Sexton, G, Whittingham, W, Shiomi, K, Omura, S, Byrne, B, Cecchini, G, Iwata, S. (2006) Structural and computational analysis of the quinone-binding site of complex II (succinate-ubiquinone oxidoreductase): a mechanism of electron transfer and proton conduction during ubiquinone reduction. (2006) J. Biol. Chem. 281(11) 7309 – 7316
2. Mirza, O, Guan, L, Verner, G, Iwata, S, Kaback, HR. Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY. (2006) EMBO J. 25(6) 1177 - 1183
3. Makyio, H, Iino, R, Ikeda, C, Imamura, H, Tamakoshi, M, Iwata, M, Stock, D, Bernal, RA, Carpenter, EP, Yoshida, M, Yokoyama, K, Iwata, S. (2005) Structure of a central stalk subunit F of prokaryotic V-type ATPase/synthase from Thermus thermophilus, EMBO J. 24(22) 3974 – 3983
4. Ferreira, KN, Iverson, TM, Maghlaoui, K, Barber, J, Iwata, S. Architecture of the photosynthetic oxygen-evolving center (2004) Science 303(5665) 1831 - 1838
5. Abramson J, Smirnova I, Kasho V, Verner G, Kaback HR, Iwata S. (2003) Structure and mechanism of the lactose permease of Escherichia coli Science 301(5633) 610-615