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Argonne National Laboratory's Structural Biology Center Contributes Major New Structure of Membrane Protein
Published: September 19, 2001
Posted: October 18, 2001

A multi-institutional international team has used the Advanced Photon Source (APS) at Argonne National Laboratory (ANL) to solve for the first time the structure of an integrin. Integrins are proteins found in cell membranes that control many cellular processes and serve as a channel through which viruses can enter and infect cells. These proteins have proven extremely difficult to isolate and crystallize in order to carry out determination of their three-dimensional structures. The results are reported in Science online on September 7, 2001, and will shortly appear in the print version of this journal. The integrin studied by the group is thought to have a significant function in tumor growth and may be involved in enabling infection by the viruses responsible for AIDS and foot-and-mouth disease. The structure of the protein is complicated, with twelve domains arranged in the shape of a propeller. Thanks to the new structural information, new drugs that bind the protein can be designed that may block uptake of viruses into cells or delay growth of tumors by preventing cells from building new blood vessels to support the tumors. The team included scientists at Merck in Germany, who isolated and purified samples of the protein, at Massachusetts General Hospital and Harvard Medical School in Boston, who crystallized the protein and refined the structure, and at the BER-funded Structural Biology Center at ANL, who carried out the crystallographic experiments at their beamline at the APS.

Contact: Roland Hirsch, SC-73, 3-9009
Topic Areas:

  • Research Area: Structural Biology, Biomolecular Characterization and Imaging
  • Research Area: Structural Biology Infrastructure

Division: SC-33.2 Biological Systems Science Division, BER
      (formerly SC-73 Medical Sciences Division, OBER)


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