J Michael Sauder - Structural genomics of protein phosphatases

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  Publication Details (including relevant citation   information):

  J Struct Funct Genomics (2007) 8: 121-140.

  Almo SC, Bonanno JB, Sauder JM, Emtage S, Dilorenzo TP,   Malashkevich V, Wasserman SR, Swaminathan S, Eswaramoorthy S,   Agarwal R, Kumaran D, Madegowda M, Ragumani S, Patskovsky Y,   Alvarado J, Ramagopal UA, Faber-Barata J, Chance MR, Sali A,   Fiser A, Zhang ZY, Lawrence DS, Burley SK

  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.

  Address (URL): http://www.ncbi.nlm.nih.gov/pubmed/18058037

 

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