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Metabolic and rare disease Lab

At present his research at CIC bioGUNE is devoted to understand the molecular mechanisms by which structural motifs known as "CBS domains" regulate the activity of proteins with biomedical interest, including cystathionine beta-synthase, the enzyme from which these motifs were baptized. His group has wide expertise in Macromolecular X-ray crystallography and in Biophysical techniques applied to elucidate the regulation of two families of proteins: (i) human cystathionine b-synthase, and (ii) the Cyclin M (CNNM) family of magnesium transporters. Mutations within the amino acid sequence of these proteins are linked to different rare diseases, like Homocystinuria or Familial Hypomagnesemia, but also to more prevalent pathologies, that include cancer and cognitive disorders like Alzheimer disease or Down Syndrome. Among his most sound results is the long-sought crystal structure of full-length human cystathionine b-synthase in its “basal” and its “activated” state, as well as the three-dimensional structure of the intracellular region of the human CNNM2 transporter.

Main Research Lines: 
CBS domains