2017 Fiscal Year Final Research Report
Structural basis of substrate recognition and regulation by ADAM/ADAMTS family proteinases
Project/Area Number |
26440040
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Structural biochemistry
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Research Institution | National Cardiovascular Center Research Institute |
Principal Investigator |
TAKEDA Soichi 国立研究開発法人国立循環器病研究センター, 研究所, 室長 (80332279)
|
Project Period (FY) |
2014-04-01 – 2018-03-31
|
Keywords | プロテアーゼ / タンパク質間相互作用 / マルチドメイン構造 / 細胞間シグナリング / 基質認識機構 / X線結晶構造解析 |
Outline of Final Research Achievements |
ADAM and ADMTS family of proteins are extracellular modular metalloproteinases composing of several functional domains other than the catalytic domain. ADAM/ADAMTS proteinases play key roles in development and morphogenesis, and are also involved in numerous disease conditions. Most ADAMs are type I membrane proteins whereas all ADAMTS members are soluble proteinases. ADAMs and ADAMTSs share functional domains other than the catalytic domain. The purpose of this study is to elucidate structure-function relationships of ADAM/ADAMTS family proteinases. We have solved crystal structures of the zymogen form of VAP2, a snake venom ADAM, and revealed the common architecture of the pro-domain of ADAM/ADAMTS family proteinases.
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Free Research Field |
構造生物学
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