Telephone: 6316 2857
- BSc, MSc and PhD, Universitat Autònoma de Barcelona (Catalonia, Spain)
- Postdoctoral. University of Essex, UK
- Postdoctoral. University of Cambridge,UK
Membrane proteins constitute a third of all proteins and are involved in almost every process in the cell, mediating communication between cell compartments, and between the cellular inside and the outside world. Some of these proteins are the richest receptor targets for drug discovery, and account for the activity of nearly 60% of all prescription drugs. The properties of these molecules are determined by their transmembrane domains, typically α-helices, which show a fascinating capacity for promiscuity.
To understand how these proteins work it is essential to combine structural and functional information. My interest is at present focused on the activity modulation of
- Ion channels of viral origin
- Signal transduction systems.
Ion channels. Controlling permeability of membranes is a strategy for treating disease. A classical example is the use of amantadine, an M2 proton channel-blocker, to treat influenza A infection. Although the use of amantadine was suggested more than 30 years ago, only recently high resolution structural details of the mechanism of this inhibition, and amantadine resistance, have emerged. In recent years, viral ion channels such as poliovirus 2B, alphavirus 6K, HIV-1 Vpu, influenza virus M2, or SARS E protein (SCoV E), some of which are possible pharmaceutical targets, have been named collectively as ‘viroporins’.
Signal transduction. Transmembrane α-helices are also used to transfer information across different cell compartments, or across the plasma membrane. Examples of this can be found in integrins or in receptor tyrosine kinases (RTK), like the fibroblast growth factor receptor (FGFR). Mutations in the transmembrane domain of these molecules lead to unregulated signaling.