2hxp

<StructureSection load='2hxp' size='340' side='right' caption='[[2hxp]], [[Resolution|resolution]] 1.83&Aring;' scene=''>

<table><tr><td colspan='2'>[[2hxp]] is a 1 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=2HXP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HXP FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DUSP9, MKP4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></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=2hxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hxp OCA], [http://pdbe.org/2hxp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hxp RCSB], [http://www.ebi.ac.uk/pdbsum/2hxp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hxp ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/2hxp TOPSAN]</span></td></tr>

[[http://www.uniprot.org/uniprot/DUS9_HUMAN DUS9_HUMAN]] Inactivates MAP kinases. Has a specificity for the ERK family.

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== 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.

 

== References ==

[[Category: Human]]

[[Category: Protein-tyrosine-phosphatase]]

[[Category: Burley, S K]]

[[Category: Eswaramoorthy, S]]

[[Category: Madegowda, M]]

[[Category: Structural genomic]]

[[Category: Swaminathan, S]]

[[Category: PSI, Protein structure initiative]]