2hy3

<StructureSection load='2hy3' size='340' side='right' caption='[[2hy3]], [[Resolution|resolution]] 2.60&Aring;' scene=''>

<table><tr><td colspan='2'>[[2hy3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HY3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HY3 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hy3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hy3 OCA], [http://pdbe.org/2hy3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hy3 RCSB], [http://www.ebi.ac.uk/pdbsum/2hy3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hy3 ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/2hy3 TOPSAN]</span></td></tr>

== Function ==

[[http://www.uniprot.org/uniprot/PTPRG_HUMAN PTPRG_HUMAN]] Possesses tyrosine phosphatase activity.<ref>PMID:19167335</ref>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

Structural genomics of protein phosphatases.,Almo SC, Bonanno JB, Sauder JM, Emtage S, Dilorenzo TP, Malashkevich V, Wasserman SR, Swaminathan S, Eswaramoorthy S, Agarwal R, Kumaran D, Madegowda M, Ragumani S, Patskovsky Y, Alvarado J, Ramagopal UA, Faber-Barata J, Chance MR, Sali A, Fiser A, Zhang ZY, Lawrence DS, Burley SK J Struct Funct Genomics. 2007 Sep;8(2-3):121-40. Epub 2007 Dec 5. PMID:18058037<ref>PMID:18058037</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2hy3" style="background-color:#fffaf0;"></div>

*[[Tyrosine phosphatase|Tyrosine phosphatase]]

[[Category: Human]]

[[Category: Protein-tyrosine-phosphatase]]

[[Category: Bera, A]]

[[Category: Burley, S K]]

[[Category: Freeman, J C]]

[[Category: Jin, X]]

[[Category: Min, T]]

[[Category: Mu, H]]

[[Category: Structural genomic]]

[[Category: Reyes, C]]

[[Category: Sauder, J M]]

[[Category: Shapiro, L]]

[[Category: Smith, D]]

[[Category: Wasserman, S R]]

[[Category: Twisted mixed beta-sheets flanked by {alpha}-helice]]