Substrate binding mechanism of heparan sulfate N-sulfotransferase
| Project/Area Number |
12680611
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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 | KYUSHU UNIVERSITY (2001)
Osaka University (2000) |
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Principal Investigator |
KAKUTA Yoshimitsu Kyushu University, 大学院・農学研究院, 助教授 (00314360)
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| Project Period (FY) |
2000 – 2001
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 2001: ¥1,700,000 (Direct Cost: ¥1,700,000)
Fiscal Year 2000: ¥1,900,000 (Direct Cost: ¥1,900,000)
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| Keywords | heparan sulfate / sulfotransferase / X線結晶構造解析 / 硫酸転移反応 / 基質特異性 |
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| Research Abstract |
Heparan sulfates are the complex chains of sulfated glycosaminoglycans. Heparan sulfate chains are ubiquitously present as proteoglycans on cell surfaces and in extracellular matrix. They have been increasingly implicated in various biological processes including cell growth, cell differentiation, blood coagulation, and viral and bacterial infections.
Heparan sulfate sulfotransferase (NST) catalyzes transfer of the 5'- sulfuryl group of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the amino group of heparan sulfate. We determined 2A^^゜ resolution structure of NST-PAPS complex. The structure indicate that residues Lys614, Lys833, Lys676 and GLU642 play an important role for PAPS binding and enzyme activity.
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Report
(3 results)
Research Products
(8 results)
