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Structure and molecular behavior of the second magnetorecepter candidate protein ISCA1

https://repo.qst.go.jp/records/77251
https://repo.qst.go.jp/records/77251
6694c9d6-9c90-41f2-b0d3-7395f9a3414d
Item type 会議発表用資料 / Presentation(1)
公開日 2019-10-29
タイトル
タイトル Structure and molecular behavior of the second magnetorecepter candidate protein ISCA1
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_c94f
資源タイプ conference object
アクセス権
アクセス権 metadata only access
アクセス権URI http://purl.org/coar/access_right/c_14cb
著者 Arai, Shigeki

× Arai, Shigeki

WEKO 821465

Arai, Shigeki

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Shimizu, Rumi

× Shimizu, Rumi

WEKO 821466

Shimizu, Rumi

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Adachi, Motoyasu

× Adachi, Motoyasu

WEKO 821467

Adachi, Motoyasu

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Ajito, Satoshi

× Ajito, Satoshi

WEKO 821468

Ajito, Satoshi

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Hirai, Mitsuhiro

× Hirai, Mitsuhiro

WEKO 821469

Hirai, Mitsuhiro

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Arai, Shigeki

× Arai, Shigeki

WEKO 821470

en Arai, Shigeki

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Shimizu, Rumi

× Shimizu, Rumi

WEKO 821471

en Shimizu, Rumi

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Adachi, Motoyasu

× Adachi, Motoyasu

WEKO 821472

en Adachi, Motoyasu

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抄録
内容記述タイプ Abstract
内容記述 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.
会議概要(会議名, 開催地, 会期, 主催者等)
内容記述タイプ Other
内容記述 3rd QST International Symposium
発表年月日
日付 2019-12-04
日付タイプ Issued
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