11月1日（金曜日）に、University of Texas Southwestern Medical Center (USA)でResearch Scientistとして活躍されている内川瑛美子博士をお招きして、化学科主催・リーディング⼤学院推進センター共催で講演会を開催します。
内川氏は、本学博士後期課程在学時にストラスブール大学に留学し、2011年3月博士後期課程を修了、お茶の水女子大学から博士（理学）ならびにストラスブール大学からPhD in Aspects Moléculaires et Cellulaires de la Biologieの共同学位を取得され、その後フランス、続いて米国で研究を続けておられます。
みなさまの積極的な参加をお待ちしております。
| 日時 |
|---|
| 2019年11月 1日（金曜日）16:00-17:30 |
| 場所 |
| お茶の水女子大学 理学部1号館4階 化学第二講義室（414室） |
| 講演者 |
|
内川 瑛美子 博士 Research Scientist University of Texas Southwestern Medical Center (USA) |
| テーマ |
| cryo-EM structure reveals the activation mechanism of Insulin Receptor クライオ電子顕微鏡を用いたインスリン受容体構造が解き明かす受容体活性化メカニズム |
| 要旨 |
| Activation mechanism of the insulin receptor revealed by cryo-EM structure of the fully liganded receptor–ligand complex The insulin receptor (INSR) is a receptor tyrosine kinase (RTK) that plays essential roles in glucose metabolism. Dysregulation of IR signaling leads to metabolic syndromes, such as diabetes. Because of its therapeutic potential, INSR have been studied more than 50 years. Despite numerous amount of studies, the activation mechanism of INSR is only partially understood. The activation model where insulin bridges two INSR is generally accepted even if there is no structural evidence. Furthermore, the binding stoichiometry of insulin and INSR has not been determined. Biochemical studies indicated that insulin bind to two district binding sites on INSR by using two distinct interfaces but the second insulin binding site on the receptor remained elusive. Until now, the reported cryo-electron microscopy structures of INSR were unable to identify the location of the second binding site. Last year, we determined the high-resolution insulin bound INSR structure (3.1 Å resolution) using cryo-electron microscopy and finally identified the second insulin binding site. The complex configuration was different from the generally accepted bridging model. We determined four insulins in our structures and insulins does not bridge the INSR using two distinct interface. Insulins simply bind to the two binding sites using two interfaces. We proceeded to confirm the second binding site using mutagenesis and cell-based assays to confirm its significance. Our discovery provides a basis for understanding the activation kinetics of INSR and opens new research directions for the exploration of diabetes treatment. |
| 対象 |
| 本学の学生・教職員の方ならどなたでも参加いただけます。 |
| お問合せ／連絡先 |
|
お茶の水女子大学 リーディング大学院推進センター tel:03-5978-5775 e-mail: |
