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Title: Structural genomics : keeping up with expanding knowledge of the protein universe.

Abstract

No abstract prepared.

Authors:
; ; ; ; ; ;
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE Office of Science (SC); National Institutes of Health (NIH)
OSTI Identifier:
928663
Report Number(s):
ANL/BIO/JA-61340
TRN: US200811%%286
DOE Contract Number:
DE-AC02-06CH11357
Resource Type:
Journal Article
Resource Relation:
Journal Name: Curr. Opinion Struct. Biol.; Journal Volume: 17; Journal Issue: 2007
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; PROTEINS; UNIVERSE; BIOLOGY

Citation Formats

Grabowski, M., Joachimiak, A., Otwinowski, Z., Minor, W., Biosciences Division, Univ. of Virginia, and UT Southwestern Medical Center at Dallas. Structural genomics : keeping up with expanding knowledge of the protein universe.. United States: N. p., 2007. Web. doi:10.1016/j.sbi.2007.06.003.
Grabowski, M., Joachimiak, A., Otwinowski, Z., Minor, W., Biosciences Division, Univ. of Virginia, & UT Southwestern Medical Center at Dallas. Structural genomics : keeping up with expanding knowledge of the protein universe.. United States. doi:10.1016/j.sbi.2007.06.003.
Grabowski, M., Joachimiak, A., Otwinowski, Z., Minor, W., Biosciences Division, Univ. of Virginia, and UT Southwestern Medical Center at Dallas. Mon . "Structural genomics : keeping up with expanding knowledge of the protein universe.". United States. doi:10.1016/j.sbi.2007.06.003.
@article{osti_928663,
title = {Structural genomics : keeping up with expanding knowledge of the protein universe.},
author = {Grabowski, M. and Joachimiak, A. and Otwinowski, Z. and Minor, W. and Biosciences Division and Univ. of Virginia and UT Southwestern Medical Center at Dallas},
abstractNote = {No abstract prepared.},
doi = {10.1016/j.sbi.2007.06.003},
journal = {Curr. Opinion Struct. Biol.},
number = 2007,
volume = 17,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}
  • The United States National Institutes of Health (NIH) Protein Structure Initiative (PSI) is a joint government, university, and industry effort, organized and supported by the National Institute of General Medical Sciences (NIGMS), and aimed at reducing the costs in increasing the speed of protein structure determination. Its long-range goal is to make the three-dimensional atomic-level structures of most proteins in nature easily obtainable from knowledge of their corresponding DNA sequences (http://www.nigms.gov/psi). It is the primary U.S. component of a broad international effort in structural genomics, involving at least 20 projects throughout the world. The PSI is now in its fourthmore » year. Nine PSI pilot research centers have been funded to explore the feasibility and impact of genomic scale protein structure analysis. To date, over 500 3D protein structures, providing the first structural representatives for hundreds of protein domain families, have been completed and deposited by the NIH centers into the public Protein Data Bank. In addition, new technologies for protein sample production, data organization, and structure analysis by X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy have been developed. These technologies increase the efficiency of protein structure determination both for structural genomics and for the broader structural biology community. Although progress has been substantial, PSI pilot research centers have identified a number of important bottlenecks that need to be solved to meet the goals of the program. For example, it is now accepted that a major challenge to high-throughput protein structure determination is the fact that for some 70% of targeted proteins, it is difficult to produce protein samples and crystals suitable for structural analysis. In an effort to facilitate an effective exchange of developments and advancements between pilot centers, the NIGMS organized a workshop on gene cloning, protein expression and purification in March 2002. The scope of a subsequent workshop in April 2003 was expanded to include high-throughput methods for protein crystallization. Protein production for structural genomics comprises aspects of target protein selection, cloning and expression of recombinant proteins, cell-culture fermentation, isotopic enrichment with selenium for X-ray crystallography and/or stable isotopes for NMR studies, purification, analytical characterization, growing X-ray quality crystals and the process of organizing these results and reagents into databases and reagent libraries, as well as issues associated with distributing these reagents to the broader community.« less
  • No abstract prepared.
  • No abstract prepared.
  • The New York SGX Research Center for Structural Genomics (NYSGXRC) of the NIGMS Protein Structure Initiative (PSI) has applied its high-throughput X-ray crystallographic structure determination platform to systematic studies of all human protein phosphatases and protein phosphatases from biomedically-relevant pathogens. To date, the NYSGXRC has determined structures of 21 distinct protein phosphatases: 14 from human, 2 from mouse, 2 from the pathogen Toxoplasma gondii, 1 from Trypanosoma brucei, the parasite responsible for African sleeping sickness, and 2 from the principal mosquito vector of malaria in Africa, Anopheles gambiae. These structures provide insights into both normal and pathophysiologic processes, including transcriptionalmore » regulation, regulation of major signaling pathways, neural development, and type 1 diabetes. In conjunction with the contributions of other international structural genomics consortia, these efforts promise to provide an unprecedented database and materials repository for structure-guided experimental and computational discovery of inhibitors for all classes of protein phosphatases.« less