TY - JOUR
T1 - Structural genomics of protein phosphatases
AU - Almo, Steven C.
AU - Bonanno, Jeffrey B.
AU - Sauder, J. Michael
AU - Emtage, Spencer
AU - Dilorenzo, Teresa P.
AU - Malashkevich, Vladimir
AU - Wasserman, Steven R.
AU - Swaminathan, S.
AU - Eswaramoorthy, Subramaniam
AU - Agarwal, Rakhi
AU - Kumaran, Desigan
AU - Madegowda, Mahendra
AU - Ragumani, Sugadev
AU - Patskovsky, Yury
AU - Alvarado, Johnjeff
AU - Ramagopal, Udupi A.
AU - Faber-Barata, Joana
AU - Chance, Mark R.
AU - Sali, Andrej
AU - Fiser, Andras
AU - Zhang, Zhong Yin
AU - Lawrence, David S.
AU - Burley, Stephen K.
PY - 2007/9/1
Y1 - 2007/9/1
N2 - 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.
AB - 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.
KW - NYSGXRC
KW - Phosphatase
KW - Structural genomics
KW - X-ray crystallography
UR - http://www.scopus.com/inward/record.url?scp=37449032927&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=37449032927&partnerID=8YFLogxK
U2 - 10.1007/s10969-007-9036-1
DO - 10.1007/s10969-007-9036-1
M3 - Review article
C2 - 18058037
AN - SCOPUS:37449032927
VL - 8
SP - 121
EP - 140
JO - Journal of Structural and Functional Genomics
JF - Journal of Structural and Functional Genomics
SN - 1345-711X
IS - 2-3
ER -