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Binding of trifluoperazine to apocalmodulin revealed by a combination of small‐angle X‐ray scattering and nuclear magnetic resonance
Author(s) -
Matsushima Norio,
Hayashi Nobuhiro,
Watanabe Noriko,
Jinbo Yuji,
Izumi Yoshinobu
Publication year - 2007
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s0021889807002117
Subject(s) - small angle x ray scattering , crystallography , scattering , chemistry , trifluoperazine , titration , materials science , nuclear magnetic resonance , calmodulin , physics , organic chemistry , optics , calcium
Small‐angle X‐ray scattering (SAXS) and nuclear magnetic resonance (NMR) studies were performed to investigate the binding of trifluoperazine (TFP) to Ca 2+ ‐free calmodulin (apoCaM) with N‐ and C‐terminal globular domains connected by a linker. The SAXS and NMR measurements were taken throughout the titration of TFP. The SAXS analyses indicate that the binding of TFP induces structural changes from a dumbbell shape to a compact globular shape in solution. The formation of the complete globular structure requires 5.0 added equivalents of TFP. An analysis of NMR chemical‐shift changes indicates that the C‐terminal domain of apoCaM is involved in the binding of TFP. The SAXS and NMR data reflect the high structural flexibility of apoCaM.