2q5e: Difference between revisions
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==Crystal structure of human carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2== | ==Crystal structure of human carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2== | ||
<StructureSection load='2q5e' size='340' side='right' caption='[[2q5e]], [[Resolution|resolution]] 2.51Å' scene=''> | <StructureSection load='2q5e' size='340' side='right' caption='[[2q5e]], [[Resolution|resolution]] 2.51Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTDSP2, NIF2, OS4 ([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">CTDSP2, NIF2, OS4 ([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=2q5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q5e OCA], [http://pdbe.org/2q5e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2q5e RCSB], [http://www.ebi.ac.uk/pdbsum/2q5e PDBsum], [http://www.topsan.org/Proteins/NYSGXRC/2q5e 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=2q5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q5e OCA], [http://pdbe.org/2q5e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2q5e RCSB], [http://www.ebi.ac.uk/pdbsum/2q5e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2q5e ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/2q5e TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 2q5e" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2q5e" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:39, 18 October 2017
Crystal structure of human carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2Crystal structure of human carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2
Structural highlights
Function[CTDS2_HUMAN] Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residues repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation. Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells. May contribute to the development of sarcomas.[1] [2] 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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