2G59

Crystal Structure of the Catalytic Domain of Protein Tyrosine Phosphatase from Homo sapiens

Summary for 2G59

• Entry DOI: 10.2210/pdb2g59/pdb
• Descriptor: Receptor-type tyrosine-protein phosphatase O, PHOSPHATE ION (3 entities in total)
• Functional Keywords: protein tyrosine phosphatase, dephosphorylation, structural genomics, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, hydrolase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 70075.25

Authors

Kumaran, D.,Swaminathan, S.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2006-02-22, release date: 2006-03-14, Last modification date: 2023-08-30)

Primary citation

Almo, S.C.,Bonanno, J.B.,Sauder, J.M.,Emtage, S.,Dilorenzo, T.P.,Malashkevich, V.,Wasserman, S.R.,Swaminathan, S.,Eswaramoorthy, S.,Agarwal, R.,Kumaran, D.,Madegowda, M.,Ragumani, S.,Patskovsky, Y.,Alvarado, J.,Ramagopal, U.A.,Faber-Barata, J.,Chance, M.R.,Sali, A.,Fiser, A.,Zhang, Z.Y.,Lawrence, D.S.,Burley, S.K.
Structural genomics of protein phosphatases.
J.Struct.Funct.Genom., 8:121-140, 2007

PubMed 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.

PubMed: 18058037
DOI: 10.1007/s10969-007-9036-1

Experimental method

X-RAY DIFFRACTION (2.19 Å)