Journal of Structural and Functional Genomics

, Volume 8, Issue 2, pp 121–140

Structural genomics of protein phosphatases

Authors

    • Albert Einstein College of Medicine
  • Jeffrey B. Bonanno
    • Albert Einstein College of Medicine
  • J. Michael Sauder
    • SGX Pharmaceuticals, Inc.
  • Spencer Emtage
    • SGX Pharmaceuticals, Inc.
  • Teresa P. Dilorenzo
    • Albert Einstein College of Medicine
  • Vladimir Malashkevich
    • Albert Einstein College of Medicine
  • Steven R. Wasserman
    • SGX Pharmaceuticals, Inc.
  • S. Swaminathan
    • Brookhaven National Laboratory
  • Subramaniam Eswaramoorthy
    • Brookhaven National Laboratory
  • Rakhi Agarwal
    • Brookhaven National Laboratory
  • Desigan Kumaran
    • Brookhaven National Laboratory
  • Mahendra Madegowda
    • Brookhaven National Laboratory
  • Sugadev Ragumani
    • Brookhaven National Laboratory
  • Yury Patskovsky
    • Albert Einstein College of Medicine
  • Johnjeff Alvarado
    • Albert Einstein College of Medicine
  • Udupi A. Ramagopal
    • Albert Einstein College of Medicine
  • Joana Faber-Barata
    • Albert Einstein College of Medicine
  • Mark R. Chance
    • Case Western Reserve University
  • Andrej Sali
    • University of California at San Francisco
  • Andras Fiser
    • Albert Einstein College of Medicine
  • Zhong-yin Zhang
    • Indiana University School of Medicine
  • David S. Lawrence
    • University of North Carolina at Chapel Hill
    • SGX Pharmaceuticals, Inc.
Article

DOI: 10.1007/s10969-007-9036-1

Cite this article as:
Almo, S.C., Bonanno, J.B., Sauder, J.M. et al. J Struct Funct Genomics (2007) 8: 121. doi:10.1007/s10969-007-9036-1

Abstract

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 transcriptional 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.

Keywords

Structural genomics Phosphatase NYSGXRCX-ray crystallography

Copyright information

© Springer Science+Business Media B.V. 2007