Biophysical Society announces new and notable symposiu...( High-resolution Structure of the Hu...)

High-resolution Structure of the Human beta2-adrenergic Receptor.
Vadim Cherezov, The Scripps Research Institute.

Dr. Cherezov has solved the first high-resolution structure of a human G protein-coupled receptor with a diffusible ligand. This breakthrough represents the initial step in elucidating structural aspects of the ligand binding specifity and the mechanism of signal transduction by this diverse family of human druggable receptors. This is a major breakthrough that could only have been realized with the conjunction of the in meso method for membrane protein crystallization, a novel synchrotron X-ray beam and a suitably engineered protein. The target protein is of great biological and medical relevance.

Determining the Architectures of Macromolecular Assemblies by Integrating Spatial Restraints from Proteomic Data.
Frank Alber, University of Sounther California.

Dr. Alber has devised an integrative approach to determine the architectures of macromolecular assemblies from diverse biophysical and proteomic data. By applying this approach, he and his colleagues have determined the configuration of the 456 proteins in the nuclear pore complex (NPC) and gained insights into the assembly's evolution and architectural principles. The NPC controls the access of macromolecules in and out of the cell nucleus. The approach can, in principle, be applied to resolve the architectures of many other macromolecular complexes.

For more information or press credentials, contact Ellen Weiss at eweiss@biophysics org, or stop by the Society office located in the Room 103A of the Long Beach convention center.

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