神谷成敏

研究者氏名	神谷成敏
	カミヤナルトシ
URL
所属	兵庫県立大学
部署	情報科学研究科
職名	特任教授
科研費研究者番号	80420462
J-Global ID	201801005421048355

研究分野

ライフサイエンス / 生物物理学 /

論文

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The Effect of Conformational Flexibility on Binding Free Energy Estimation between Kinases and Their Inhibitors

Mitsugu Araki Narutoshi Kamiya Miwa Sato Masahiko Nakatsui Takatsugu Hirokawa Yasushi Okuno

JOURNAL OF CHEMICAL INFORMATION AND MODELING 56(12) 2445-2456 2016年12月 [査読有り]

Accurate prediction of binding affinities of drug candidates to their targets remains challenging because of protein flexibility in solution. Conformational flexibility of the ATP-binding site in the CDK2 and ERK2 kinases was identified using mole...

Revisiting antibody modeling assessment for CDR-H3 loop

Hiroshi Nishigami Narutoshi Kamiya Haruki Nakamura

PROTEIN ENGINEERING DESIGN & SELECTION 29(11) 477-484 2016年11月 [査読有り]

The antigen-binding site of antibodies, also known as complementarity-determining region (CDR), has hypervariable sequence properties. In particular, the third CDR loop of the heavy chain, CDR-H3, has such variability in its sequence, length, and ...

Model Building of Antibody-Antigen Complex Structures Using GBSA Scores

Noriko Shimba Narutoshi Kamiya Haruki Nakamura

JOURNAL OF CHEMICAL INFORMATION AND MODELING 56(10) 2005-2012 2016年10月 [査読有り]

Structure prediction of antibody-antigen complexes, which involves molecular docking to generate decoys that are ranked using a scoring function, is an important approach in the design of antibody drugs and biosensors. However, it is not easy to e...

Elastic properties of dynein motor domain obtained from all-atom molecular dynamics simulations

Narutoshi Kamiya Tadaaki Mashimo Yu Takano Takahide Kon Genji Kurisu Haruki Nakamura

PROTEIN ENGINEERING DESIGN & SELECTION 29(8) 317-325 2016年8月 [査読有り]

Dyneins are large microtubule motor proteins that convert ATP energy to mechanical power. High-resolution crystal structures of ADP-bound cytoplasmic dynein have revealed the organization of the motor domain, comprising the AAA(+) ring, the linker...

Structure of the Entire Stalk Region of the Dynein Motor Domain

Yosuke Nishikawa Takuji Oyama Narutoshi Kamiya Takahide Kon Yoko Y. Toyoshima Haruki Nakamura Genji Kurisu

JOURNAL OF MOLECULAR BIOLOGY 426(19) 3232-3245 2014年9月 [査読有り]

Dyneins are large microtubule-based motor complexes that power a range of cellular processes including the transport of organelles, as well as the beating of cilia and flagella. The motor domain is located within the dynein heavy chain and compris...