2000 Fiscal Year Final Research Report Summary
Molecular Mechanism of Target Recognition by Calmodulin
| Project/Area Number |
10450358
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| Research Category |
Grant-in-Aid for Scientific Research (B).
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
高分子構造・物性(含繊維)
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| Research Institution | Yamagata University |
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Principal Investigator |
IZUMI Yoshinobu Graduate School of Science and Engineering, Yamagata University Professor, 大学院・理工学研究科, 教授 (30002158)
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| Co-Investigator(Kenkyū-buntansha) |
JINBO Yuji Graduate School of Science and Engineering, Yamagata University, Research Associate, 大学院・理工学研究科, 助手 (40311584)
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| Project Period (FY) |
1998 – 2000
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| Keywords | Calmodulin / Myosin light chain kinase / Calcineurin / Calmodulin-dependent protein kinase I, II, IV / CAP-23 / NAP-22 / W-7 / TFP / Recognition Sequence |
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| Research Abstract |
9-1) Small-angle X-ray scattering (SAXS) was used to investigate the conformational changes of calmodulin on binding to a calmodulin-binding sequence in myosin light chain kinase, calcineurin, calmodulin-protein kinase. I, II, IV and these binding motifs were determined on the molecular level.
9-2) SAXS was used to investigate the conformational changes of calmodulin on binding to a myristoylated N-terminal nonapeptide from neuron-specific protein CAP-23/NAP-22 and the binding motif was determined on the molecular level.
9-3) SAXS was used to investigate the conformational changes of calmodulin on binding to an antagonist like W-7 and TFP and the binding motif was determined on the molecular level.
9-4) In the absence of Ca^<2+>, a new binding motif was found in the calmodulin/TFP and calmodulin/calmodulin-dependent protein kinase TV complexes.
9-5) SAXS was used to reveal the role of the central helix in calmodulin for its recognition.
9-6) SAXS with stopped-flow technique was used to reveal the kinetic conformational change of Ca^<2+>-dependent target recognition by calmodulin.
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Research Products
(13 results)
