Poly (ADP-ribose) polymerase
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
PARP1 is composed of 3 domains. Among them are the N terminal DNA-binding domain which contains <scene name='43/439963/Cv/3'>5 zinc fingers (residues 1-97, 105-206, 207-366)</scene>. The auto modification (AD) domain which contains a breast cancer 1 protein (BRCT) C-terminus domain (residues 386-485) and a WGR domain (rich in Trp, Gly and Arg) (residues 517-642). The C terminal domain which includes the catalytic domain (or PARP domain) (residues 662-1011)<ref>PMID:19372272</ref>. <scene name='43/439963/Cv/6'>A potential drug binds at the active site pocket</scene><ref>PMID:24922587</ref>. | PARP1 is composed of 3 domains. Among them are the N terminal DNA-binding domain which contains <scene name='43/439963/Cv/3'>5 zinc fingers (residues 1-97, 105-206, 207-366)</scene>. The auto modification (AD) domain which contains a breast cancer 1 protein (BRCT) C-terminus domain (residues 386-485) and a WGR domain (rich in Trp, Gly and Arg) (residues 517-642). The C terminal domain which includes the catalytic domain (or PARP domain) (residues 662-1011)<ref>PMID:19372272</ref>. <scene name='43/439963/Cv/6'>A potential drug binds at the active site pocket</scene><ref>PMID:24922587</ref>. | ||
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| + | == 3D Structures of Poly (ADP-ribose) polymerase == | ||
| + | [[Poly(ADP-ribose) polymerase 3D structures]] | ||
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</StructureSection> | </StructureSection> | ||
== 3D Structures of Poly (ADP-ribose) polymerase == | == 3D Structures of Poly (ADP-ribose) polymerase == | ||
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{{#tree:id=OrganizedByTopic|openlevels=0| | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
| - | *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; | + | *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; ART 788-1012; 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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**[[6bhv]] – hPARP 1 catalytic domain + NAD homolog<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 /> | **[[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]], [[6ghk]] – hPARP 1 catalytic domain (mutant) + inhibitor<br /> |
| + | **[[6nrf]], [[6nrg]], [[6nrh]], [[6nri]], [[6nrj]] – hPARP 1 ART domain + inhibitor<br /> | ||
**[[4xhu]] – hPARP 1 catalytic domain + protein homeless homolog<br /> | **[[4xhu]] – hPARP 1 catalytic domain + protein homeless homolog<br /> | ||
**[[4opx]], [[4oqa]], [[4oqb]] – hPARP-1 zinc fingers 1,2,3, WGR and catalytic domain + DNA<br /> | **[[4opx]], [[4oqa]], [[4oqb]] – hPARP-1 zinc fingers 1,2,3, WGR and catalytic domain + DNA<br /> | ||
| + | **[[6i8m]], [[6imt]] – cPARP-1 catalytic domain + inhibitor – chicken<br /> | ||
*Poly (ADP-ribose) polymerase 2 | *Poly (ADP-ribose) polymerase 2 | ||
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**[[3kjd]], [[3kcz]], [[4tvj]], [[4zzx]], [[4zzy]], [[5dsy]] - hPARP 2 catalytic domain + inhibitor<br /> | **[[3kjd]], [[3kcz]], [[4tvj]], [[4zzx]], [[4zzy]], [[5dsy]] - hPARP 2 catalytic domain + inhibitor<br /> | ||
**[[4pjv]] - hPARP 2 α helical and catalytic domain + inhibitor<br /> | **[[4pjv]] - hPARP 2 α helical and catalytic domain + inhibitor<br /> | ||
| + | **[[6f1k]], [[6f5b]], [[6f5f]] - hPARP 2 WGR domain + DNA<br /> | ||
**[[5d5k]] - hPARP 2 residues 1-78 + importin subunit -1 <br /> | **[[5d5k]] - hPARP 2 residues 1-78 + importin subunit -1 <br /> | ||
**[[1gs0]] - mPARP 2 catalytic domain - mouse | **[[1gs0]] - mPARP 2 catalytic domain - mouse | ||
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**[[5lx6]] - hPARP 10 catalytic domain + inhibitor<br /> | **[[5lx6]] - hPARP 10 catalytic domain + inhibitor<br /> | ||
**[[3hkv]] - hPARP 10 catalytic domain (mutant) + inhibitor<br /> | **[[3hkv]] - hPARP 10 catalytic domain (mutant) + inhibitor<br /> | ||
| + | **[[6fxi]] - hPARP-10 catalytic domain + aminobenzamide<br /> | ||
**[[2dhx]] - hPARP 10 RRM domain | **[[2dhx]] - hPARP 10 RRM domain | ||
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*Poly (ADP-ribose) polymerase 14; Domains – WWE 139-224; macro 1 708-898; macro 2 918-1115; macro 3 1208-1388; catalytic 1611-1801 | *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]], [[6g0w]] - hPARP 14 catalytic domain + inhibitor<br /> | + | **[[3goy]], [[3se2]], [[3smi]], [[3smj]], [[4f1l]], [[4f1q]], [[4py4]], [[5lxp]], [[5lyh]], [[5nqe]], [[5v7t]], [[5v7w]], [[6g0w]], [[6fym]], [[6fzm]] - 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 /> | ||
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**[[3v2b]] – hPARP-15 macro domain 2 + ADP<br /> | **[[3v2b]] – hPARP-15 macro domain 2 + ADP<br /> | ||
| - | *Poly (ADP-ribose) polymerase 16 | + | *Poly (ADP-ribose) polymerase 16 residues 5-279 |
| - | **[[4f0d]] - hPARP-16 + aminobenzamide | + | **[[4f0d]] - hPARP-16 + aminobenzamide<br /> |
| + | **[[6hxr]] - hPARP-16 + inhibitor<br /> | ||
| + | **[[6hxs]] - hPARP-16 + CABRA-NAD<br /> | ||
*Poly (ADP-ribose) polymerase | *Poly (ADP-ribose) polymerase | ||
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**[[5jti]], [[5ju5]], [[5kni]] - hTank 1 SAM domain<br /> | **[[5jti]], [[5ju5]], [[5kni]] - hTank 1 SAM domain<br /> | ||
**[[2rf5]] - hTank 1 catalytic domain (mutant)<br /> | **[[2rf5]] - hTank 1 catalytic domain (mutant)<br /> | ||
| - | **[[3udd]], [[3uh2]], [[3uh4]], [[4dvi]], [[4i9i]], [[4k4e]], [[4k4f]], [[4krs]], [[4li6]], [[4li7]], [[4li8]], [[4msg]], [[4msk]], [[4mt9]], [[4n3r]], [[4n4v]], [[4oa7]], [[4w5s]], [[4w6e]], [[4tor]], [[4u6a]], [[4uuh]], [[4uw1]], [[5ebt]], [[5ece]] - hTank 1 catalytic domain + inhibitor<br /> | + | **[[3udd]], [[3uh2]], [[3uh4]], [[4dvi]], [[4i9i]], [[4k4e]], [[4k4f]], [[4krs]], [[4li6]], [[4li7]], [[4li8]], [[4msg]], [[4msk]], [[4mt9]], [[4n3r]], [[4n4v]], [[4oa7]], [[4w5s]], [[4w6e]], [[4tor]], [[4u6a]], [[4uuh]], [[4uw1]], [[5ebt]], [[5ece]], [[6qxu]] - hTank 1 catalytic domain + inhibitor<br /> |
**[[4tos]], [[5ety]] - hTank 1 catalytic domain (mutant) + inhibitor<br /> | **[[4tos]], [[5ety]] - hTank 1 catalytic domain (mutant) + inhibitor<br /> | ||
**[[5gp7]] - hTank 1 residues 799-957 + USP25<br /> | **[[5gp7]] - hTank 1 residues 799-957 + USP25<br /> | ||
Revision as of 08:46, 25 November 2019
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3D Structures of Poly (ADP-ribose) polymerase
Updated on 25-November-2019
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
