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

Research output: Contribution to journal › Article › peer-review

47 Citations (Scopus)

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.

Original language	English
Pages (from-to)	173-177
Number of pages	5
Journal	FEBS Letters
Volume	442
Issue number	2-3
DOIs	https://doi.org/10.1016/S0014-5793(98)01637-8
Publication status	Published - 1999 Jan 15
Externally published	Yes

Keywords

Calmodulin-W-7 complex
Conformational change
Globular structure
Small-angle X-ray scattering

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/S0014-5793(98)01637-8

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title = "Evidence for calmodulin inter-domain compaction in solution induced by W-7 binding",

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.",

keywords = "Calmodulin-W-7 complex, Conformational change, Globular structure, Small-angle X-ray scattering",

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",

note = "Funding Information: We are grateful to Claude Klee for kindly providing the Xenopus calmodulin expression system. This work was supported in part by grants (to M.I.) from the Medical Research Council of Canada (MRCC) and by the Suhara foundation (to N.M.). M.I. is a Howard Hughes Medical Institute International Research Scholar. Small-angle X-ray scattering measurement was performed under approval of the Photon Factory Advisory Committee (Proposal No. 98G202). ",

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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

N1 - Funding Information: We are grateful to Claude Klee for kindly providing the Xenopus calmodulin expression system. This work was supported in part by grants (to M.I.) from the Medical Research Council of Canada (MRCC) and by the Suhara foundation (to N.M.). M.I. is a Howard Hughes Medical Institute International Research Scholar. Small-angle X-ray scattering measurement was performed under approval of the Photon Factory Advisory Committee (Proposal No. 98G202).

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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ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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