New Publication: "GPR97 triggers inflammatory processes in human neutrophils via a macromolecular complex upstream of PAR2 activation"

crystal structure of the gpr97 extracellular domain

Illustration: Crystal structure of the GPR97 extracellular domain

Neutrophils are a type of white blood cell that are part of our innate immune system. Their activities require tight regulation to avoid unwanted inflammation and autoimmune diseases. Here we show that the protein GPR97, which is found on the surface of neutrophils, plays a role in this process. It associates with a potent proteolytic protein found on neutrophils, the membrane proteinase 3 (mPR3). Together with other protein interaction partners we identified such as PAR2, this association is a key step leading to neutrophil activation. Structural/functional analysis of the GPR97 extracellular region identified two mPR3-binding domains. Both GPR97 and mPR3 are upregulated on the surface of disease-associated neutrophils, suggesting a role in pathologic inflammation.

The full article can be read at


Elena Seiradake
27th October 2022

Full list of paper authors: Trisha Gura, Amparo Acker-Palmer, Alex Kolodkin, Rob Meijers, Naoko Mizuno, Elena Seiradake, Marc Tessier-Lavigne