Title
Intrinsically Disordered Proteins: Structure, Property and Function
Organizers
Motonori Ota (Nagoya University), Hidekazu Hiroaki (Kobe University)
Synopsis
When intrinsically disordered proteins (IDPs) exist as isolated polypeptide chains under physiological conditions, they lack stable and unique tertiary structures. However, if IDPs interact with their target proteins, they will adopt well-defined structures. This very characteristic binding scheme is called as “coupled folding and binding”, and distinguishable from the classical “lock-and-key” or “induced fit” mechanisms. IDPs are mostly found in eukaryotes, localized in nucleus, and generally interact with several target proteins, playing important roles as hubs in protein-protein interaction networks. From the last year, a research project focusing on the IDPs started, and several talks were already given by the project member so far at several research meetings. In this symposium, we ask researches who are not involved in the research project, but addressing to this area, to present their recent works. We expect attendees to join active discussions, and spend exciting hours.
Speakers
・ Kei Yura (Ochanomizu University): The interwinding nature of protein-protein interfaces and its implication for protein complex formation
・ Shuichi Takeda (Nagoya University)： Regulatory mechanism of actin capping protein by an intrinsically disordered peptide CARMIL
・ Yuji Sugita (RIKEN): Molecular simulations of soft interaction between calcium pump and phospholamban
・ Mikio Kataoka (NAIST): The mechanism of induced folding of Staphylococcal nuclease: Folding before binding or binding before folding?
シンポジウムのリストへ戻る
Intrinsically Disordered Proteins: Structure, Property and Function
Organizers
Motonori Ota (Nagoya University), Hidekazu Hiroaki (Kobe University)
Synopsis
When intrinsically disordered proteins (IDPs) exist as isolated polypeptide chains under physiological conditions, they lack stable and unique tertiary structures. However, if IDPs interact with their target proteins, they will adopt well-defined structures. This very characteristic binding scheme is called as “coupled folding and binding”, and distinguishable from the classical “lock-and-key” or “induced fit” mechanisms. IDPs are mostly found in eukaryotes, localized in nucleus, and generally interact with several target proteins, playing important roles as hubs in protein-protein interaction networks. From the last year, a research project focusing on the IDPs started, and several talks were already given by the project member so far at several research meetings. In this symposium, we ask researches who are not involved in the research project, but addressing to this area, to present their recent works. We expect attendees to join active discussions, and spend exciting hours.
Speakers
・ Kei Yura (Ochanomizu University): The interwinding nature of protein-protein interfaces and its implication for protein complex formation
・ Shuichi Takeda (Nagoya University)： Regulatory mechanism of actin capping protein by an intrinsically disordered peptide CARMIL
・ Yuji Sugita (RIKEN): Molecular simulations of soft interaction between calcium pump and phospholamban
・ Mikio Kataoka (NAIST): The mechanism of induced folding of Staphylococcal nuclease: Folding before binding or binding before folding?
シンポジウムのリストへ戻る