| Project/Area Number |
08680668
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Structural biochemistry
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| Research Institution | The Tokyo Metropolitan Institute of Medical Science |
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Principal Investigator |
KAWASAKI Hiroshi Tokyo Metropolitan Institute of Med.Sci.Research scientist, 遺伝情報研究部門, 研究員 (70169704)
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| Project Period (FY) |
1996 – 1997
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| Project Status |
Completed (Fiscal Year 1997)
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| Budget Amount *help |
¥2,300,000 (Direct Cost: ¥2,300,000)
Fiscal Year 1997: ¥1,200,000 (Direct Cost: ¥1,200,000)
Fiscal Year 1996: ¥1,100,000 (Direct Cost: ¥1,100,000)
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| Keywords | calcium / calpain / protease / calpastatin / annexin / アネモシン |
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| Research Abstract |
Calpain, an itracelular calcium-dependent cystein protease, is thought to perform various physiological functions by cleaving substrate proteins to a limited extent, and altering or down-regulating their activities or functions. Altough the structural and biochemical features of calpains have been well defined, substrate specificity or substrate-recognition mechanism remains to be investigated. Calpastatin, an endogenous calpain inhibitor is distributed ubiquitously as well as calpain. Interaction between calpain and calpastatin is very specific, so this will be a good model for substrate recognition by calpain. Effects of calpastatin peptides against structural changes of calpain induced by calcium ions and other metal ions were investigated. The peptides supposed to bind at hydrophobic surface of calpain exposed by the binding of calcium ions. Crystal structure of annexin I,a substrate of calpain, was also solved. The site cleaved by calpain at N-tail of annexin I did not have enough density to build a model. The refinement is still in progress.
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