Structural biology of the intrinsically disordered region of CagA

2016 Fiscal Year Final Research Report

• Project/Area Number: 15K18495
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Structural biochemistry
• Research Institution: High Energy Accelerator Research Organization
• Principal Investigator: Suzuki Nobuhiro 大学共同利用機関法人高エネルギー加速器研究機構, 物質構造科学研究所, 研究員 (40712659)
• Research Collaborator: SENDA Toshiya ; SHIMIZU Nobutaka ; HATAKEYAMA Masanori ; TAKEUCHI Koh
• Project Period (FY): 2015-04-01 – 2017-03-31
• Keywords: ピロリ菌 / CagA / 天然変性領域

Outline of Final Research Achievements

CagA is a protein produced by Helicobacter pylori and is known to cause gastric ulcer and gastric cancer. When injected into the target cell by the bacterium, CagA interacts with many different signaling molecules and deregulate the bound targets. CagA is composed of N-terminal structured region and C-terminal intrinsically disordered region. It has been suggested that the intrinsically disordered region forms a loop like structure by intramolecularly interacting with the structured region. Here we performed solution structure analysis of this loop like structure to elucidate the significance of the structure for its function by means of NMR, SAXS, CD analyses and other structural studies with functional analysis. To be noted, CD and NMR analyses revealed that, upon intramolecular interaction between the structured region and intrinsically disordered region, the interaction site in the intrinsically disordered region formed helices likely to form helix bundles with structured region.

Free Research Field

構造生物化学