2zzc: Difference between revisions
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==Crystal structure of NADP(H):human thioredoxin reductase I== | ==Crystal structure of NADP(H):human thioredoxin reductase I== | ||
<StructureSection load='2zzc' size='340' side='right' caption='[[2zzc]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='2zzc' size='340' side='right' caption='[[2zzc]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TXNRD1, KDRF ([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">TXNRD1, KDRF ([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/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </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=2zzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zzc OCA], [http://pdbe.org/2zzc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zzc RCSB], [http://www.ebi.ac.uk/pdbsum/2zzc PDBsum]</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=2zzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zzc OCA], [http://pdbe.org/2zzc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zzc RCSB], [http://www.ebi.ac.uk/pdbsum/2zzc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zzc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 2zzc" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2zzc" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Lo, Y C]] | [[Category: Lo, Y C]] | ||
[[Category: Wang, A H.J]] | [[Category: Wang, A H.J]] | ||
[[Category: Alternative splicing]] | |||
[[Category: Cytoplasm]] | |||
[[Category: Electron transport]] | [[Category: Electron transport]] | ||
[[Category: Fad]] | [[Category: Fad]] | ||
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[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Phosphoprotein]] | [[Category: Phosphoprotein]] | ||
[[Category: Polymorphism]] | |||
[[Category: Redox-active center]] | [[Category: Redox-active center]] | ||
[[Category: Rossmann fold]] | [[Category: Rossmann fold]] | ||
Revision as of 16:32, 12 October 2017
Crystal structure of NADP(H):human thioredoxin reductase ICrystal structure of NADP(H):human thioredoxin reductase I
Structural highlights
Function[TRXR1_HUMAN] Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid.[1] [2] [3] [4] 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 PubMedTerpyridine-platinum(II) (TP-Pt(II)) complexes are known to possess DNA-intercalating activity and have been regarded as potential antitumor agents. However, their cytotoxic mechanism remains unclear. To investigate the possible mechanism, a series of TP-Pt(II) compounds were prepared and their biological activities assessed. The DNA binding activities of the aromatic thiolato[TP-Pt(II)] complexes were stronger than the aliphatic 2-hydroxylethanethiolato(2,2':6',2-terpyridine)platinum(II) [TP(HET)]. TP-Pt(II) complexes inhibited topoisomerase IIalpha or topoisomerase I activity at IC(50) values of about 5 microM and 10-20 microM, respectively, whereas the human thioredoxin reductase 1 (hTrxR1) activity was inhibited with IC(50) values in the range of 58-78 nM. At the cellular level, they possessed cytotoxicity with IC(50) values between 7 and 19 microM against HeLa cells. Additionally, using X-ray crystallography and matrix-assisted laser desorption/ionization (MALDI) mass spectrometry, we elucidated that the TP-Pt(II) complexes inhibited hTrxR1 activity by blocking its C-terminal active-site selenocysteine. Therefore, TP-Pt(II) complexes possess inhibitory activities against multiple biological targets, and they may be further studied as anticancer agents. Terpyridine-platinum(II) complexes are effective inhibitors of mammalian topoisomerases and human thioredoxin reductase 1.,Lo YC, Ko TP, Su WC, Su TL, Wang AH J Inorg Biochem. 2009 Jul;103(7):1082-92. Epub 2009 May 21. PMID:19525010[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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