BiographyNir Ben-Tal obtained his bachelor degree in Biology, Chemistry and Physics at the Hebrew University in 1988 and his Doctor of Science degree in Chemistry at the Technion, Israel Institute of Technology in 1993. He carried out his postdoctoral training in computational biophysics at Columbia University between 1993-1997. In 1997 he joined the Department of Biochemistry (now called the Department of Biochemistry and Molecular Biology) at Tel Aviv University and since 2007 he is full professor in the department. His research group, of about ten students and postdoctoral researchers, studies various aspects in computational biology with a focus on structural bioinformatics (http://ashtoret.tau.ac.il). To give an example, his laboratory predicted the 3-dimensional structure of human copper transporter 1 (hCTR1) and conducted normal mode analysis of the model structure. The calculations were used to suggest a mechanism by which hCTR1 transports copper ions one by one, keeping them under close control. Careful ion selection and regulation are essential because free copper ions are highly reactive, potentially forming harmful free radicals. His lab also develops the ConSurf web-server for the detection of functional regions by mapping evolutionary data on protein structures (http://consurf.tau.ac.il).
Computational biology, bioinformatics, computational structural biology.
Areas of Research / Professional Expertise
Nir Ben-Tal’s research focuses mostly on the general area of computational structural biology. His past research achievements, in collaboration with junior and senior scientists, have been the development of computational tools and their application to selected biological systems. Specific examples include:
• The development of the ConSurf methodology and web-server (http://consurf.tau.ac.il/) for the detection of functional regions in proteins. ConSurf provides an estimate of the evolutionary rate of each amino acid position in a protein and projects the rates on the 3D structure of the protein. Clusters of slowly evolving amino acids that are in close proximity to each other on the protein surface are often functionally important. For example, they could mediate binding to DNA, RNA, ligands or other proteins.
• The development of various computational tools for membrane protein structure prediction.
• The prediction of model structures of a homodimer of the transmembrane domain of the receptor tyrosine kinase ErbB2 (HER2) in two conformations and the suggestion that they correspond to the active and inactive states of the receptor. His team proposed a molecular mechanism for rotation-coupled activation of the receptor, thereby explaining the effect of its overexpression on kinase activity and cell transformation and the outcome of mutations, including the known neu* activating oncogenic point mutation. The proposed activation model gained support from many experimental and clinical studies, the most convincing of which were NMR studies that showed that both conformations were correct.
• The prediction of a model structure of the bacterial EmrE multi-drug membrane transporter and suggestion of a mechanism of substrate transfer. Nir Ben-Tal’s team suggested a homodimeric structure, the monomers of which were in opposite topologies in the membrane, which was controversial. Subsequent X-ray crystallography studies showed that the model structure was accurate, and very recent NMR studies support the suggested transport mechanism.
• The prediction of model structures of two human membrane sodium/proton exchangers (NHE1 and NhaA2) and suggestions of their transport mechanisms. The models inspired experimental work and are used by collaborators and others to suggest molecular interpretation of their results.
• The prediction of a C-alpha trace model and functional dynamics of the homotrimeric human copper transporter CTR1 and the suggestion of a transport mechanism.
• Suggestion of putative amino acid determinants of the emergence of the 2009 influenza A (H1N1)virus in the human population.
Doing sports, playing soccer in particular.