Alfonso Martínez de la Cruz
Alfonso Martínez de la Cruz
Phone: 4314 / 944 061 320
Address: Bizkaia Science and Technology Park,
building 800, Derio (Bizkaia)

Alfonso Martínez de la Cruz got his undergraduate degree in Chemistry from the Universidad Autónoma de Madrid, Spain (1992). He finished his PhD work at the Department of Crystallography of Institute Rocasolano (1997) under a FPI fellowship from the Spanish Ministry of Science. Afterwards, he held three post doctoral positions, first at the Max Planck Institute Für Medizinische Forschung in Heidelberg, Germany in the lab of Professors Ken Holmes and Wolfgang Kabsch, where he carried out structural studies of proteins involved in Chagas disease (March-October, 1997). His work there was done in collaboration with Prof. Luise Krauth-Siegel, at the Department of Biochemistry of the University of Heidelberg. In October 1997 he moved to USA to join Sung-Hou Kim´s lab at Univ. of California, Berkeley, granted by a Fulbright Fellowship and later by a postdoctoral contract at the Department of Chemistry of this University. His work at Berkeley focused on the nascent Structural Genomics Initiative, aimed to perform high-throughput structure determination of proteins to setup the limits of the protein fold universe. In September 2000, he returned to Spain and joined the lab of Prof. José María Mato at the Univ. of Navarra, in Pamplona, granted first by a postdoctoral fellowship and later under a contract as a Scientist at the Center for Applied Medical Research (CIMA). During his stay in Pamplona he performed structural studies on enzymes regulated by S-adenosylmethionine (AdoMet), a hub molecule of the methionine cycle, that regulates the activity of several metabolic enzymes linked to the development of human liver diseases, including liver cancer and several rare pathologies. The biological relevance and complex regulation of one of this enzymes, cystathionine beta-synthase (CBS), which is key in regulating the transsulfuration pathway in mammals, focused his attention for future studies. In January 2005, he joined CIC bioGUNE, in Bilbao, as Principal Investigator.

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.