@misc{oai:repo.qst.go.jp:00077251,
 author = {Arai, Shigeki and Shimizu, Rumi and Adachi, Motoyasu and Ajito, Satoshi and Hirai, Mitsuhiro and Arai, Shigeki and Shimizu, Rumi and Adachi, Motoyasu},
 month = {Dec},
 note = {The quantum mechanism of magnetoreception in the biological system has been mainly investigated using cryptochromes (Crys). However, the signal transduction mechanism from Cry to the nervous system and the brain has not been elucidated yet. Recently, the ISCA1 (also called MagR) protein of pigeon, fruit fly, etc. was found to interact with Cry. The pigeon Cry4/ISCA1 (pCry4/pISCA1) complex orientates along the weak magnetic field (0.4 G) under blue light [4], suggesting that ISCA1 might be a partner of Cry upon the magnetoreception reaction and/or the signal transduction. In order to elucidate the structure and molecular behavior of pISCA1, we conducted the small angle X-ray scattering (SAXS) analysis. The result indicated that pISCA1 forms two types of conformers; the rod-like type-A and the globular type-B. The type-B conformer was self-polymerized larger than octamer. Molecular modeling of the pISCA1 based on the SAXS data and the crystal structures of homologs (PDB: 2D2A, 1R94, 1X0G) suggested that Fe-S clusters bind to the interfaces between the type-B pISCA1 molecules in its oligomer. The conformational change from type-A to type-B and the subsequent self-polymerization of pISCA1 should enable to bind many Fe-S clusters that might improve the magnetomotive force of the pCry4/pISCA1 complex to orientate along the external magnetic field., 3rd QST International Symposium},
 title = {Structure and molecular behavior of the second magnetorecepter candidate protein ISCA1},
 year = {2019}
}