2HCM

Crystal structure of mouse putative dual specificity phosphatase complexed with zinc tungstate, New York Structural Genomics Consortium

2HCM の概要

• エントリーDOI: 10.2210/pdb2hcm/pdb
• 分子名称: Dual specificity protein phosphatase, TUNGSTATE(VI)ION, ZINC ION, ... (6 entities in total)
• 機能のキーワード: phosphatase, structural genomics, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, hydrolase
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18087.86

構造登録者

Patskovsky, Y.,Almo, S.C.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (登録日: 2006-06-17, 公開日: 2006-08-15, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)