Laboratory for Protein Functional and Structural Biology
- E-mail：mikako.shirouzu[at]riken.jpPlease replace [at] with @.
Establishment of a structural analysis technology platform that contributes to "life innovation" such as drug development and medical treatment.
The high-resolution structural information of proteins related to diseases shall increasingly become important for drug development leading to future individualized medicine. We plan to establish a structural analysis technology platform to contribute to "Life innovation" such as drug discovery as well as development of methods for the sample preparation of challenging proteins including membrane proteins/biomolecular complexes and for the structural analysis by cryo-electron microscopy (cryo-EM). The 3D-structural information will be used for in-silico screening/design of chemical compounds and for dynamic structural analysis toward simulation research of cell function.
cryo-EM (FEI Tecnai Arctica)
- Three-dimensional structure determination for drug development
- Development of methods for preparing difficult proteins including membrane proteins
- Structural analysis for huge complex of biomolecules by cryo-EM
Main Publications List
- Kujirai T, Ehara H, Fujino Y, et al.
Structural basis of the nucleosome transition during RNA polymerase II passage.
Science (2018) doi: 10.1126/science.aau9904
- Shigematsu H, Imasaki T, Doki C, et al.
Structural insight into microtubule stabilization and kinesin inhibition by Tau-family MAPs.
The Journal of Cell Biology (2018) doi: 10.1083/jcb.201711182
Shima T, Morikawa M, Kaneshiro J, et al.
Kinesin-binding–triggered conformation switching of microtubules contributes to polarized transport.
The Journal of Cell Biology 217(12).4164-4183 (2018) doi: 10.1083/jcb.201711178
Ohbayashi N, Murayama K, Kato-Murayama M, et al.
Structural Basis for the Inhibition of Cyclin G-Associated Kinase by Gefitinib.
ChemistryOpen 7(9). 721-727 (2018) doi: 10.1002/open.201800177
Kasuya G, Nakane T, Yokoyama T, et al.
Cryo-EM structures of the human volume-regulated anion channel LRRC8.
Nature Structural & Molecular Biology 25 (9). 797-804 (2018) doi: 10.1038/s41594-018-0109-6
Yamagata A, Miyazaki Y, Yokoi N, et al.
Structural basis of epilepsy-related ligand–receptor complex LGI1–ADAM22.
Nature communications 9(1). 1546 (2018) doi: 10.1038/s41467-018-03947-w
Matsuda T, Ito T, Takemoto C, et al.
Cell-free synthesis of functional antibody fragments to provide a structural basis for antibody-antigen interaction.
PLoS One 13(2) e0193158 (2018) doi:10.1371/journal.pone.0193158
- Hosaka T, Okazaki M, Kimura-Someya T, et al.
Crystal structural characterization reveals novel oligomeric interactions of human voltage-dependent anion channel 1.
Protein Science 26(9). 1749-1758 (2017) doi:10.1002/pro.3211
Shinoda T, Shinya N, Ito K, et al.
Structural basis for disruption of claudin assembly in tight junctions by an enterotoxin.
Scientific Reports 6. 33632 (2016) doi:10.1038/srep33632
Masuda M, Uno Y, Ohbayashi N, et al.
TNIK inhibition abrogates colorectal cancer stemness.
Nature Communications 7. 12586 (2016) doi:10.1038/ncomms12586