2p8e: Difference between revisions
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==Crystal structure of the serine/threonine phosphatase domain of human PPM1B== | ==Crystal structure of the serine/threonine phosphatase domain of human PPM1B== | ||
<StructureSection load='2p8e' size='340' side='right' caption='[[2p8e]], [[Resolution|resolution]] 1.82Å' scene=''> | <StructureSection load='2p8e' size='340' side='right' caption='[[2p8e]], [[Resolution|resolution]] 1.82Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPM1B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPM1B ([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/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </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=2p8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p8e OCA], [http://pdbe.org/2p8e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2p8e RCSB], [http://www.ebi.ac.uk/pdbsum/2p8e PDBsum], [http://www.topsan.org/Proteins/NYSGXRC/2p8e TOPSAN]</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=2p8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p8e OCA], [http://pdbe.org/2p8e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2p8e RCSB], [http://www.ebi.ac.uk/pdbsum/2p8e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2p8e ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/2p8e TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Revision as of 12:20, 18 October 2017
Crystal structure of the serine/threonine phosphatase domain of human PPM1BCrystal structure of the serine/threonine phosphatase domain of human PPM1B
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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