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2PBN

Crystal structure of the human tyrosine receptor phosphate gamma

Summary for 2PBN
Entry DOI10.2210/pdb2pbn/pdb
Related2HY3
DescriptorReceptor-type tyrosine-protein phosphatase gamma, SULFATE ION (3 entities in total)
Functional Keywordsstructural genomics, hydrolase, psi-2, protein structure initiative, new york sgx research center for structural genomics, nysgxrc
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight36185.00
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 (1.7 Å)
Structure validation

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数据于2025-06-11公开中

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