Monitoring intramolecular conformational rearrangements.
Using advanced fluorescence spectroscopy approaches, such as tmFRET, we probe subtle structural changes, which are at the base of the functional regulation of any protein.
EAG channel outline.
As founding members of the KCNH voltage gated potassium channel family, EAG channels usually express in the CNS. However, EAG transcripts have been found in every cancerous tissue tested to date. EAG channels are tetramers, with four subunits surrounding a centrally located pore. The illustration shows a side view of the channel, with a single subunit highlighted as a cartoon showing its transmembrane domain (green) and intracellular C-linker and CNBHD (red and blue, respectively). The amino-terminal EAG domain is not shown (adapted from Haitin Y, Nat. Chem. Biol., 2014).
Structural Physiology Triangle.
Our lab strives to provide and enhance the mechanistic understanding of basic molecular processes. Our focal points revolve around the regulatory processes involving ion channels and the mechanisms of contributing to their diverse function. To do so, we use an array of cutting edge approaches, which include structural biology, electrophysiology, fluorescence and cellular-based assays, to establish a comprehensive, multi-tiered picture illustrating the contribution of ion channels to immune and cancer cells various activities.
Images of protein crystals.
Protein crystals are usually grown under vapor diffusion, which facilitates slow sample concentration and nucleation. Optimized protein crystals are used for X-ray diffraction experiments, with the goal of atomic structure determination.
The intracellular complex of a KCNH channel.
A top view of the complex between the EAG domain (green) and the CNBHD (blue) is shown. Ca2+-CaM carboxy-terminal low-affinity binding domain is indicated in red (adapted from Haitin et al., Nature, 2013).