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2NV5

Crystal structure of a C-terminal phosphatase domain of Rattus norvegicus ortholog of human protein tyrosine phosphatase, receptor type, D (PTPRD)

Summary for 2NV5
Entry DOI10.2210/pdb2nv5/pdb
Descriptorprotein-tyrosine-phosphatase (2 entities in total)
Functional Keywordsphosphatase, structural genomics, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, hydrolase
Biological sourceRattus norvegicus (Norway rat)
Total number of polymer chains3
Total formula weight103037.23
Authors
Primary citationAlmo, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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