Structure determination of oligomeric membrane protein involved in forming membrane vesicles and elucidation of the regulation mechanism

2016 Fiscal Year Final Research Report

• Project/Area Number: 26440034
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Structural biochemistry
• Research Institution: Tokyo University of Science (2016); University of Shizuoka (2014-2015)
• Principal Investigator: YOKOYAMA HIDESHI 東京理科大学, 薬学部生命創薬科学科, 准教授 (70433208)
• Project Period (FY): 2014-04-01 – 2017-03-31
• Keywords: 膜結合プロテアーゼ / ストマチン / OBドメイン / Ｘ線結晶構造

Outline of Final Research Achievements

In humans, an absence of stomatin is associated with a form of hemolytic anemia known as hereditary stomatocytosis. In this study, I tried to elucidate how the partner protein STOPP (STomatin Operon Partner Protein) regulates the oligomeric protein stomatin. By X-ray crystallography, I elucidated that the protease domain of STOPP could form a different dimeric structure, and that the OB (Oligonucleotide Binding) domain of STOPP could assemble into 12-24 mer multimers based on a dimer as a basic unit. This result indicates that the OB domain functions as a scaffold protein to form the multimeric assembly of STOPP and stomatin. In the future, I want to elucidate the mechanism how hereditary stomatocytosis is developed.

Free Research Field

タンパク質構造生物学