Structural basis of substrate recognition and regulation by ADAM/ADAMTS family proteinases

2017 Fiscal Year Final Research Report

• Project/Area Number: 26440040
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Structural biochemistry
• 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.

Free Research Field

構造生物学