Isabelle Baconguis, Ph.D.
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Lab Phone: info coming soon
Isabelle Baconguis graduated from the University of Pennsylvania with a B.A. in Biochemistry in 2005. She remained at the University of Pennsylvania for two years studying glutamate receptors. She joined the Neuroscience Graduate Program at OHSU in 2007. During her doctoral research at the Vollum Institute, she studied acid sensing ion channels (ASICs), members of the superfamily of amiloride-sensitive and Na+-selective trimeric ion channels. Using a combination of x-ray crystallography and electrophysiology, she exploited toxin-dependent modulation of ASIC function to elaborate molecular mechanisms of gating, selectivity and ion channel block. She joined the Vollum Insitute as a Vollum Fellow in 2013.
Summary of Current Research
The Baconguis lab is pursuing atomic-resolution mechanisms of Na+-selective and voltage-independent ion channels involved in a spectrum of processes ranging from synaptic transmission to regulation of salt homeostasis. We are especially interested in how detection of different stimuli, such as the binding of ligands or regio-specific proteolysis, is coupled to the opening of a Na+-selective transmembrane pore. The current focus of the lab is to develop molecular mechanisms of heteromeric channel assembly, channel gating and ion selectivity. The lab further seeks to map the binding sites of modulators with the long-term goal of providing blueprints for rational design of novel therapeutic agents for the treatment of diseases that include hypertension and cystic fibrosis. We employ diverse yet complementary biophysical and biochemical approaches with an emphasis on x-ray crystallography and electrophysiology.
Baconguis I, Hattori M, Gouaux E. (2013) Unanticipated parallels in architecture and mechanism between ATP-gated P2X receptors and acid sensing ion channels. Curr. Opin. Struct. Biol. 23:277-284.
Baconguis I, Gouaux E. (2012) Structural plasticity and dynamic selectivity of acid-sensing ion channel-spider toxin complexes. Nature 489:400-405.