Poly (ADP-ribose) polymerase
From Proteopedia
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<StructureSection load='4hhy' size='350' side='right' caption='Human glycosylated plasminogen complex with acetate, bicarbonate, K+ (purple) and Cl- (green) ions (PDB entry [[4hhy]])' scene=''> | <StructureSection load='4hhy' size='350' side='right' caption='Human glycosylated plasminogen complex with acetate, bicarbonate, K+ (purple) and Cl- (green) ions (PDB entry [[4hhy]])' scene=''> | ||
__TOC__ | __TOC__ | ||
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{{#tree:id=OrganizedByTopic|openlevels=0| | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
- | *Poly (ADP-ribose) polymerase 1 | + | *Poly (ADP-ribose) polymerase 1; Domains – zinc finger 1 2-96; zinc finger 2 105-206; zinc finger 3 216-366; BRCT 389-487; WGR 517-642; catalytic 662-1101 |
**[[3od8]], [[3oda]] – hPARP 1 zinc finger 1 + DNA – human<br /> | **[[3od8]], [[3oda]] – hPARP 1 zinc finger 1 + DNA – human<br /> | ||
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**[[2le0]] - PARP-1 BRCT domain – rat - NMR<br /> | **[[2le0]] - PARP-1 BRCT domain – rat - NMR<br /> | ||
**[[3u9h]] – hPARP-1 catalytic domain + nicotinamide<br /> | **[[3u9h]] – hPARP-1 catalytic domain + nicotinamide<br /> | ||
- | **[[1uk0]], [[1uk1]], [[4gv7]], [[1wok]], [[4hhy]], [[4hhz]], [[2rd6]], [[4r5w]], [[4r6e]], [[4rv6]], [[4und]], [[4uxb]], [[4zzz]], [[5a00]], [[5ds3]], [[5ha9]] – hPARP-1 catalytic domain + inhibitor<br /> | + | **[[6bhv]] – hPARP 1 catalytic domain + NAD homolog<br /> |
+ | **[[1uk0]], [[1uk1]], [[4gv7]], [[1wok]], [[4hhy]], [[4hhz]], [[2rd6]], [[4r5w]], [[4r6e]], [[4rv6]], [[4und]], [[4uxb]], [[4zzz]], [[5a00]], [[5ds3]], [[5ha9]], [[5xsu]], [[5xst]], [[5xsr]] – hPARP-1 catalytic domain + inhibitor<br /> | ||
**[[3l3l]], [[3l3m]], [[3gn7]], [[4l6s]], [[5kpn]], [[5kpo]], [[5kpp]], [[5kpq]], [[5wrq]], [[5wry]], [[5wrz]], [[5ws0]], [[5ws1]], [[5wtc]] – hPARP 1 catalytic domain (mutant) + inhibitor<br /> | **[[3l3l]], [[3l3m]], [[3gn7]], [[4l6s]], [[5kpn]], [[5kpo]], [[5kpp]], [[5kpq]], [[5wrq]], [[5wry]], [[5wrz]], [[5ws0]], [[5ws1]], [[5wtc]] – hPARP 1 catalytic domain (mutant) + inhibitor<br /> | ||
**[[4xhu]] – hPARP 1 catalytic domain + protein homeless homolog<br /> | **[[4xhu]] – hPARP 1 catalytic domain + protein homeless homolog<br /> | ||
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**[[2pqf]] - hPARP-12 catalytic domain + inhibitor | **[[2pqf]] - hPARP-12 catalytic domain + inhibitor | ||
- | *Poly (ADP-ribose) polymerase 14 | + | *Poly (ADP-ribose) polymerase 14; Domains – WWE 139-224; macro 1 708-898; macro 2 918-1115; macro 3 1208-1388; catalytic 1611-1801 |
- | **[[3goy]], [[3se2]], [[3smi]], [[3smj]], [[4f1l]], [[4f1q]], [[4py4]], [[5lxp]], [[5lyh]], [[5nqe]], [[5v7t]], [[5v7w]] - hPARP 14 catalytic domain + inhibitor<br /> | + | **[[3goy]], [[3se2]], [[3smi]], [[3smj]], [[4f1l]], [[4f1q]], [[4py4]], [[5lxp]], [[5lyh]], [[5nqe]], [[5v7t]], [[5v7w]], [[6g0w]] - hPARP 14 catalytic domain + inhibitor<br /> |
**[[3q6z]] - hPARP-14 macro domain 1+ ADPR<br /> | **[[3q6z]] - hPARP-14 macro domain 1+ ADPR<br /> | ||
**[[3q71]] - hPARP-14 macro domain 2+ ADPR<br /> | **[[3q71]] - hPARP-14 macro domain 2+ ADPR<br /> | ||
+ | **[[5o2d]] - hPARP-14 macro domain 2 (mutant) + inhibitor<br /> | ||
**[[3vfq]], [[4d86]] - hPARP-14 macro domain 1+2 + ADPR<br /> | **[[3vfq]], [[4d86]] - hPARP-14 macro domain 1+2 + ADPR<br /> | ||
**[[4abk]] - hPARP-14 macro domain 3+ ADPR<br /> | **[[4abk]] - hPARP-14 macro domain 3+ ADPR<br /> | ||
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**[[4f0e]] - hPARP-15 catalytic domain + ligand<br /> | **[[4f0e]] - hPARP-15 catalytic domain + ligand<br /> | ||
**[[3gey]] - hPARP-15 catalytic domain + inhibitor<br /> | **[[3gey]] - hPARP-15 catalytic domain + inhibitor<br /> | ||
+ | **[[6ek3]] - hPARP-15 catalytic domain (mutant) + inhibitor<br /> | ||
**[[3v2b]] – hPARP-15 macro domain 2 + ADP<br /> | **[[3v2b]] – hPARP-15 macro domain 2 + ADP<br /> | ||
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**[[4f0d]] - hPARP-16 + aminobenzamide | **[[4f0d]] - hPARP-16 + aminobenzamide | ||
- | *Poly (ADP-ribose) polymerase | + | *Poly (ADP-ribose) polymerase |
**[[1a26]] – cPARP catalytic domain +carba-NAD – chicken<br /> | **[[1a26]] – cPARP catalytic domain +carba-NAD – chicken<br /> | ||
**[[2paw]] - cPARP catalytic domain<br /> | **[[2paw]] - cPARP catalytic domain<br /> | ||
**[[2pax]], [[4pax]], [[3pax]], [[1pax]], [[1efy]] - cPARP catalytic domain + inhibitor<br /> | **[[2pax]], [[4pax]], [[3pax]], [[1pax]], [[1efy]] - cPARP catalytic domain + inhibitor<br /> | ||
+ | **[[5ngo]] – AtPARP Rcd1 PARP domain residues 269-460 – ''Arabidopsis thaliana''<br /> | ||
+ | **[[5n9q]] – AtPARP Rcd1 residues 468-567 <br /> | ||
*Tankyrases 1 (SAM domain 1018-1093; catalytic domain 1093-1325) | *Tankyrases 1 (SAM domain 1018-1093; catalytic domain 1093-1325) | ||
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**[[5jhq]] - hTank 1 residues 174-649 + peptide<br /> | **[[5jhq]] - hTank 1 residues 174-649 + peptide<br /> | ||
- | *Tankyrase 2 (SAM domain 867-940; catalytic domain 946-1113; C-terminal domain 1114-1162) | + | *Tankyrase 2 or PARP 5b (SAM domain 867-940; catalytic domain 946-1113; C-terminal domain 1114-1162) |
**[[5jrt]] - hTank 2 SAM domain<br /> | **[[5jrt]] - hTank 2 SAM domain<br /> | ||
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**[[3kr7]] - hTank 2 catalytic domain<br /> | **[[3kr7]] - hTank 2 catalytic domain<br /> | ||
**[[4hki]] - hTank 2 catalytic + C terminal domains<br /> | **[[4hki]] - hTank 2 catalytic + C terminal domains<br /> | ||
- | **[[3mhk]], [[3mhj]], [[3p0n]], [[3p0p]], [[3p0q]], [[3kr8]], [[3kr8]], [[3u9y]], [[3ua9]], [[3w51]], [[4avu]], [[4avw]], [[4bfp]], [[4bj9]], [[4bjb]], [[4bjc]], [[4bs4]], [[4bu3]], [[4bu5]], [[4bu6]], [[4bu7]], [[4bu8]], [[4bu9]], [[4bua]], [[4bud]], [[4bue]], [[4buf]], [[4bui]], [[4bus]], [[4but]], [[4buu]], [[4buv]], [[4buw]], [[4bux]], [[4buy]], [[4hyf]], [[4iue]], [[4j1z]], [[4j21]], [[4j22]], [[4j3l]], [[4j3m]], [[4m7b]], [[4pml]], [[4pnl]], [[4pnm]], [[4pnn]], [[4pnq]], [[4pnr]], [[4pns]], [[4pnt]], [[4tju]], [[4tjw]], [[4tjy]], [[4tk0]], [[4tk5]], [[4tkf]], [[4tkg]], [[4tki]], [[5aku]], [[5akw]], [[5al1]], [[5al2]], [[5al3]], [[5al4]], [[5al5]], [[4ufu]], [[4uhg]], [[4ui3]], [[4ui4]], [[4ui5]], [[4ui6]], [[4ui7]], [[4ui8]], [[4uvl]], [[4uvn]], [[4uvo]], [[4uvp]], [[4uvs]], [[4uvt]], [[4uvu]], [[4uvv]], [[4uvw]], [[4uvx]], [[4uvy]], [[4uvz]], [[4ux4]], [[4w5i]], [[5adq]], [[5adr]], [[5ads]], [[5adt]], [[5aeh]] - hTank 2 catalytic domain+ inhibitor<br /> | + | **[[3mhk]], [[3mhj]], [[3p0n]], [[3p0p]], [[3p0q]], [[3kr8]], [[3kr8]], [[3u9y]], [[3ua9]], [[3w51]], [[4avu]], [[4avw]], [[4bfp]], [[4bj9]], [[4bjb]], [[4bjc]], [[4bs4]], [[4bu3]], [[4bu5]], [[4bu6]], [[4bu7]], [[4bu8]], [[4bu9]], [[4bua]], [[4bud]], [[4bue]], [[4buf]], [[4bui]], [[4bus]], [[4but]], [[4buu]], [[4buv]], [[4buw]], [[4bux]], [[4buy]], [[4hyf]], [[4iue]], [[4j1z]], [[4j21]], [[4j22]], [[4j3l]], [[4j3m]], [[4m7b]], [[4pml]], [[4pnl]], [[4pnm]], [[4pnn]], [[4pnq]], [[4pnr]], [[4pns]], [[4pnt]], [[4tju]], [[4tjw]], [[4tjy]], [[4tk0]], [[4tk5]], [[4tkf]], [[4tkg]], [[4tki]], [[5aku]], [[5akw]], [[5al1]], [[5al2]], [[5al3]], [[5al4]], [[5al5]], [[4ufu]], [[4uhg]], [[4ui3]], [[4ui4]], [[4ui5]], [[4ui6]], [[4ui7]], [[4ui8]], [[4uvl]], [[4uvn]], [[4uvo]], [[4uvp]], [[4uvs]], [[4uvt]], [[4uvu]], [[4uvv]], [[4uvw]], [[4uvx]], [[4uvy]], [[4uvz]], [[4ux4]], [[4w5i]], [[5adq]], [[5adr]], [[5ads]], [[5adt]], [[5aeh]], [[5owt]], [[5ows]] - hTank 2 catalytic domain+ inhibitor<br /> |
- | **[[4hkk]], [[4hkn]], [[4hl5]], [[4hlf]], [[4hlg]], [[4hlh]], [[4hlk]], [[4hlm]], [[4hmh]], [[4kzl]], [[4kzq]], [[4kzu]], [[4l09]], [[4l0b]], [[4l0i]], [[4l0s]], [[4l0t]], [[4l0v]], [[4l10]], [[4l2f]], [[4l2g]], [[4l2k]], [[4l31]], [[4l32]], [[4l33]], [[4l34]], [[5c5p]], [[5c5q]], [[5c5r]], [[5dcz]], [[5fpf]], [[5fpg]] - hTank 2 catalytic and C terminal domains + inhibitor<br /> | + | **[[4hkk]], [[4hkn]], [[4hl5]], [[4hlf]], [[4hlg]], [[4hlh]], [[4hlk]], [[4hlm]], [[4hmh]], [[4kzl]], [[4kzq]], [[4kzu]], [[4l09]], [[4l0b]], [[4l0i]], [[4l0s]], [[4l0t]], [[4l0v]], [[4l10]], [[4l2f]], [[4l2g]], [[4l2k]], [[4l31]], [[4l32]], [[4l33]], [[4l34]], [[5c5p]], [[5c5q]], [[5c5r]], [[5dcz]], [[5fpf]], [[5fpg]], [[5nxe]], [[5nwg]], [[5nwd]], [[5nwc]], [[5nwb]] [[5nvh]], [[5nvf]], [[5nve]], [[5nvc]], [[5nut]], [[5nt4]], [[5nt0]], [[5nsx]], [[5nsp]], [[5nob]], [[4ufy]] - hTank 2 catalytic and C terminal domains + inhibitor<br /> |
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] |
Revision as of 08:54, 26 August 2018
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3D Structures of Poly (ADP-ribose) polymerase
Updated on 26-August-2018
References
- ↑ Shall S, de Murcia G. Poly(ADP-ribose) polymerase-1: what have we learned from the deficient mouse model? Mutat Res. 2000 Jun 30;460(1):1-15. PMID:10856830
- ↑ Dantzer F, Giraud-Panis MJ, Jaco I, Ame JC, Schultz I, Blasco M, Koering CE, Gilson E, Menissier-de Murcia J, de Murcia G, Schreiber V. Functional interaction between poly(ADP-Ribose) polymerase 2 (PARP-2) and TRF2: PARP activity negatively regulates TRF2. Mol Cell Biol. 2004 Feb;24(4):1595-607. PMID:14749375
- ↑ Beck C, Robert I, Reina-San-Martin B, Schreiber V, Dantzer F. Poly(ADP-ribose) polymerases in double-strand break repair: focus on PARP1, PARP2 and PARP3. Exp Cell Res. 2014 Nov 15;329(1):18-25. doi: 10.1016/j.yexcr.2014.07.003. Epub, 2014 Jul 10. PMID:25017100 doi:http://dx.doi.org/10.1016/j.yexcr.2014.07.003
- ↑ Yu M, Schreek S, Cerni C, Schamberger C, Lesniewicz K, Poreba E, Vervoorts J, Walsemann G, Grotzinger J, Kremmer E, Mehraein Y, Mertsching J, Kraft R, Austen M, Luscher-Firzlaff J, Luscher B. PARP-10, a novel Myc-interacting protein with poly(ADP-ribose) polymerase activity, inhibits transformation. Oncogene. 2005 Mar 17;24(12):1982-93. PMID:15674325 doi:http://dx.doi.org/1208410
- ↑ Karlberg T, Klepsch M, Thorsell AG, Andersson CD, Linusson A, Schuler H. Structural Basis for Lack of ADP-Ribosyltransferase Activity in Poly(ADP-Ribose) Polymerase-13/Zinc Finger Antiviral Protein. J Biol Chem. 2015 Jan 29. pii: jbc.M114.630160. PMID:25635049 doi:http://dx.doi.org/10.1074/jbc.M114.630160
- ↑ Barbarulo A, Iansante V, Chaidos A, Naresh K, Rahemtulla A, Franzoso G, Karadimitris A, Haskard DO, Papa S, Bubici C. Poly(ADP-ribose) polymerase family member 14 (PARP14) is a novel effector of the JNK2-dependent pro-survival signal in multiple myeloma. Oncogene. 2013 Sep 5;32(36):4231-42. doi: 10.1038/onc.2012.448. Epub 2012 Oct 8. PMID:23045269 doi:http://dx.doi.org/10.1038/onc.2012.448
- ↑ Cook BD, Dynek JN, Chang W, Shostak G, Smith S. Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeres. Mol Cell Biol. 2002 Jan;22(1):332-42. PMID:11739745
- ↑ Rios J, Puhalla S. PARP inhibitors in breast cancer: BRCA and beyond. Oncology (Williston Park). 2011 Oct;25(11):1014-25. PMID:22106552
- ↑ Altmeyer M, Messner S, Hassa PO, Fey M, Hottiger MO. Molecular mechanism of poly(ADP-ribosyl)ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites. Nucleic Acids Res. 2009 Jun;37(11):3723-38. doi: 10.1093/nar/gkp229. Epub 2009, Apr 16. PMID:19372272 doi:http://dx.doi.org/10.1093/nar/gkp229
- ↑ Patel MR, Bhatt A, Steffen JD, Chergui A, Murai J, Pommier Y, Pascal JM, Trombetta LD, Fronczek FR, Talele TT. Discovery and Structure-Activity Relationship of Novel 2,3-Dihydrobenzofuran-7-carboxamide and 2,3-Dihydrobenzofuran-3(2H)-one-7-carboxamide Derivatives as Poly(ADP-ribose)polymerase-1 Inhibitors. J Med Chem. 2014 Jun 25. PMID:24922587 doi:http://dx.doi.org/10.1021/jm5002502