Evidence for calmodulin inter-domain compaction in solution induced by W-7 binding

Masanori Osawa; Shigeo Kuwamoto; Yoshinobu Izumi; Kyoko L. Yap; Mitsuhiko Ikura; Tadao Shibanuma; Hisayuki Yokokura; Hiroyoshi Hidaka; Norio Matsushima

doi:10.1016/S0014-5793(98)01637-8

Evidence for calmodulin inter-domain compaction in solution induced by W-7 binding

Masanori Osawa, Shigeo Kuwamoto, Yoshinobu Izumi, Kyoko L. Yap, Mitsuhiko Ikura, Tadao Shibanuma, Hisayuki Yokokura, Hiroyoshi Hidaka, Norio Matsushima

研究成果: Article

42 引用（Scopus）

抜粋

Small-angle X-ray scattering and nuclear magnetic resonance were used to investigate the structural change of calcium-bound calmodulin (Ca²⁺/CaM) in solution upon binding to its antagonist, N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W-7). The radius of gyration was 17.4±0.3 A for Ca²⁺/CaM-W-7 with a molar ratio of 1:5 and 20.3±0.7 A for Ca²⁺/CaM. Comparison of the radius of gyration and the pair distance distribution function of the Ca²⁺/CaM-W-7 complex with those of other complexes indicates that binding of two W-7 molecules induces a globular shape for Ca²⁺/CaM, probably caused by an inter-domain compaction. The results suggest a tendency for Ca²⁺/CaM to form a globular structure in solution, which is inducible by a small compound like W-7. Copyright (C) 1999 Federation of European Biochemical Societies.

元の言語	English
ページ（範囲）	173-177
ページ数	5
ジャーナル	FEBS Letters
巻	442
発行部数	2-3
DOI	https://doi.org/10.1016/S0014-5793(98)01637-8
出版物ステータス	Published - 1999 1 15
外部発表	Yes

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

文献にアクセス

10.1016/S0014-5793(98)01637-8

フィンガープリント Evidence for calmodulin inter-domain compaction in solution induced by W-7 binding' の研究トピックを掘り下げます。これらはともに一意のフィンガープリントを構成します。

これを引用

Osawa, M., Kuwamoto, S., Izumi, Y., Yap, K. L., Ikura, M., Shibanuma, T., Yokokura, H., Hidaka, H., & Matsushima, N. (1999). Evidence for calmodulin inter-domain compaction in solution induced by W-7 binding. FEBS Letters, 442(2-3), 173-177. https://doi.org/10.1016/S0014-5793(98)01637-8

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abstract = "Small-angle X-ray scattering and nuclear magnetic resonance were used to investigate the structural change of calcium-bound calmodulin (Ca2+/CaM) in solution upon binding to its antagonist, N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W-7). The radius of gyration was 17.4±0.3 A for Ca2+/CaM-W-7 with a molar ratio of 1:5 and 20.3±0.7 A for Ca2+/CaM. Comparison of the radius of gyration and the pair distance distribution function of the Ca2+/CaM-W-7 complex with those of other complexes indicates that binding of two W-7 molecules induces a globular shape for Ca2+/CaM, probably caused by an inter-domain compaction. The results suggest a tendency for Ca2+/CaM to form a globular structure in solution, which is inducible by a small compound like W-7. Copyright (C) 1999 Federation of European Biochemical Societies.",

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author = "Masanori Osawa and Shigeo Kuwamoto and Yoshinobu Izumi and Yap, {Kyoko L.} and Mitsuhiko Ikura and Tadao Shibanuma and Hisayuki Yokokura and Hiroyoshi Hidaka and Norio Matsushima",

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doi = "10.1016/S0014-5793(98)01637-8",

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T1 - Evidence for calmodulin inter-domain compaction in solution induced by W-7 binding

AU - Osawa, Masanori

AU - Kuwamoto, Shigeo

AU - Izumi, Yoshinobu

AU - Yap, Kyoko L.

AU - Ikura, Mitsuhiko

AU - Shibanuma, Tadao

AU - Yokokura, Hisayuki

AU - Hidaka, Hiroyoshi

AU - Matsushima, Norio

PY - 1999/1/15

Y1 - 1999/1/15

N2 - Small-angle X-ray scattering and nuclear magnetic resonance were used to investigate the structural change of calcium-bound calmodulin (Ca2+/CaM) in solution upon binding to its antagonist, N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W-7). The radius of gyration was 17.4±0.3 A for Ca2+/CaM-W-7 with a molar ratio of 1:5 and 20.3±0.7 A for Ca2+/CaM. Comparison of the radius of gyration and the pair distance distribution function of the Ca2+/CaM-W-7 complex with those of other complexes indicates that binding of two W-7 molecules induces a globular shape for Ca2+/CaM, probably caused by an inter-domain compaction. The results suggest a tendency for Ca2+/CaM to form a globular structure in solution, which is inducible by a small compound like W-7. Copyright (C) 1999 Federation of European Biochemical Societies.

AB - Small-angle X-ray scattering and nuclear magnetic resonance were used to investigate the structural change of calcium-bound calmodulin (Ca2+/CaM) in solution upon binding to its antagonist, N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W-7). The radius of gyration was 17.4±0.3 A for Ca2+/CaM-W-7 with a molar ratio of 1:5 and 20.3±0.7 A for Ca2+/CaM. Comparison of the radius of gyration and the pair distance distribution function of the Ca2+/CaM-W-7 complex with those of other complexes indicates that binding of two W-7 molecules induces a globular shape for Ca2+/CaM, probably caused by an inter-domain compaction. The results suggest a tendency for Ca2+/CaM to form a globular structure in solution, which is inducible by a small compound like W-7. Copyright (C) 1999 Federation of European Biochemical Societies.

KW - Calmodulin-W-7 complex

KW - Conformational change

KW - Globular structure

KW - Small-angle X-ray scattering

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