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NIH Grants $30M to 7 Protein Structure Groups

NEW YORK, Sept 26 – The US National Institutes of Health said Tuesday it had awarded seven structural proteomics projects with a total of $30 million, as part of its five-year, $150 million Protein Structure Initiative.

The winners of the grants, most of whom represent large regional consortiums, are as follows:

The New York Structural Genomics Research Consortium is comprised of five New York City area institutes. The project expects to solve several hundred protein structures from humans and model organisms ranging from bacteria to humans. Stephen Burley of Rockefeller University is the project’s principal investigator.

The Midwest Center for Structural Genomics, a consortium of seven institutes, seeks to reduce the average cost to determine a protein structure from $100,000 to $20,000. The group will select protein targets from three kingdoms of life (Eukarya, Archaea, and Bacteria), with an emphasis on previously unknown folds and on proteins from disease-causing organisms. Andrzej Joachimiak of Argonne National Laboratory is the principal investigator.

The Structural Genomic Center aims to speed up structure determination by X-ray crystallography. It will focus on two closely related bacteria, Mycoplasma genitalium and Mycoplasma pneumoniae , with extremely small genomes to study proteins essential for independent life. The former contains the smallest genome of any free-living organism and infects the human genital and respiratory tracts. The latter causes a form of pneumonia. Sung-Hou Kim of Lawrence Berkeley National Laboratory is principal investigator.

The Northeast Structural Genomics Consortium is a collaboration of researchers in New Jersey, New York, Connecticut, Washington State, and Ontario, Canada that will target proteins from various model organisms--including the fruit fly, yeast, and the roundworm--and related human proteins. Gaetano Montelione of Rutgers University is the principal investigator.

Scientists in six countries have formed the TB Structural Genomics Consortium to determine and analyze the structures of about 400 proteins from Mycobacterium tuberculosis . The group seeks to optimize high-throughput structure determination and anticipates that this information will lead to the design of new and improved drugs and vaccines for tuberculosis. Thomas Terwilliger of Los Alamos National Laboratory is the principal investigator.

The Southeast Collaboratory for Structural Genomics, with its core in Georgia and Alabama, will analyze part of the human genome and the entire genomes of two representative organisms--the roundworm Caenorhabditis elegans and its more primitive microbial ancestor, Pyrococcus furiosus . The group emphasizes technology development, especially for automated crystallography and NMR techniques. Bi-Cheng Wang of the University of Georgia is the principal investigator.

The Joint Center for Structural Genomics, centered in California, is developing high-throughput methods for protein production, crystallization, and structure determination. It will initially also focus on novel structures from C. elegans and on human proteins thought to be involved in cell signaling. It will also determine the structures of similar proteins from other organisms to ensure the inclusion of the greatest number of unique protein folds. Ian Wilson of the Scripps Research Institute is principal investigator.

The protein initiative aims to speed up the pace of uncovering protein structures.

“In 50 years we’ve produced roughly 1,000 unique structures,” said John Norvell, the initiative’s director. “It’s not going real fast.”

The centers will begin their work by organizing all known proteins into structural, or fold, families based on their genetic sequences. They will then determine the structure of one or more proteins from each family, for a total of about 10,000 protein structures in 10 years. This information will form the foundation of a public resource linking sequence, structural, and functional information. It will also allow scientists to use gene sequences to predict the approximate structures of all other proteins.

“The goal of each of these centers is to increase the rate at which structures can be done,” said Norvell. “We hope at the end of the five-year grant period, each one of them will be solving between 100 and 200 structures a year.”

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