2r0b
From Proteopedia
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==Crystal structure of human tyrosine phosphatase-like serine/threonine/tyrosine-interacting protein== | ==Crystal structure of human tyrosine phosphatase-like serine/threonine/tyrosine-interacting protein== | ||
- | <StructureSection load='2r0b' size='340' side='right' caption='[[2r0b]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='2r0b' size='340' side='right'caption='[[2r0b]], [[Resolution|resolution]] 1.60Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2r0b]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2r0b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R0B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R0B FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2r0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r0b OCA], [https://pdbe.org/2r0b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r0b RCSB], [https://www.ebi.ac.uk/pdbsum/2r0b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r0b ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/2r0b TOPSAN]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/STYX_HUMAN STYX_HUMAN] Catalytically inactive phosphatase. Acts as a nuclear anchor for MAPK1/MAPK3 (ERK1/ERK2). Modulates cell-fate decisions and cell migration by spatiotemporal regulation of MAPK1/MAPK3 (ERK1/ERK2). Seems to play a role in spermiogenesis (By similarity). |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2r0b ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2r0b ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <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. | ||
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- | 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> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 2r0b" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
- | [[Category: Almo | + | [[Category: Large Structures]] |
- | [[Category: Bain | + | [[Category: Almo SC]] |
- | [[Category: Bonanno | + | [[Category: Bain KT]] |
- | [[Category: Burley | + | [[Category: Bonanno JB]] |
- | [[Category: Freeman | + | [[Category: Burley SK]] |
- | [[Category: Iizuka | + | [[Category: Freeman J]] |
- | + | [[Category: Iizuka M]] | |
- | [[Category: Romero | + | [[Category: Romero R]] |
- | [[Category: Sauder | + | [[Category: Sauder JM]] |
- | [[Category: Smith | + | [[Category: Smith D]] |
- | [[Category: Wasserman | + | [[Category: Wasserman S]] |
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Current revision
Crystal structure of human tyrosine phosphatase-like serine/threonine/tyrosine-interacting protein
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Categories: Homo sapiens | Large Structures | Almo SC | Bain KT | Bonanno JB | Burley SK | Freeman J | Iizuka M | Romero R | Sauder JM | Smith D | Wasserman S