4l7p

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m (Protected "4l7p" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4l7p| PDB=4l7p | SCENE= }}
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===Human artd3 (parp3) - catalytic domain in complex with inhibitor ME0395===
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{{ABSTRACT_PUBMED_24188023}}
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The entry 4l7p is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/PARP3_HUMAN PARP3_HUMAN]] Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. May link the DNA damage surveillance network to the mitotic fidelity checkpoint. Negatively influences the G1/S cell cycle progression without interfering with centrosome duplication. Binds DNA. May be involved in the regulation of PRC2 and PRC3 complex-dependent gene silencing.<ref>PMID:16924674</ref>
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Authors: Karlberg, T., Thorsell, A.G., Lindgren, A.E.G., Ekblad, T., Spjut, S., Andersson, C.D., Weigelt, J., Linusson, A., Elofsson, M., Schuler, H.
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==About this Structure==
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[[4l7p]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L7P OCA].
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Description: Human artd3 (parp3) -catalytic domain in complex with inhibitor ME0395
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==Reference==
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<ref group="xtra">PMID:024188023</ref><references group="xtra"/><references/>
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[[Category: Andersson, C D.]]
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[[Category: Ekblad, T.]]
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[[Category: Elofsson, M.]]
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[[Category: Karlberg, T.]]
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[[Category: Lindgren, A E.G.]]
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[[Category: Linusson, A.]]
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[[Category: Schuler, H.]]
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[[Category: Spjut, S.]]
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[[Category: Thorsell, A G.]]
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[[Category: Weigelt, J.]]
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[[Category: Adp-ribosylation]]
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[[Category: Diphtheria toxin like adp-ribose trasnferase]]
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[[Category: Transferase]]
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[[Category: Transferase-transferase inhibitor complex]]

Revision as of 17:17, 19 February 2014

Template:STRUCTURE 4l7p

Contents

Human artd3 (parp3) - catalytic domain in complex with inhibitor ME0395

Template:ABSTRACT PUBMED 24188023

Function

[PARP3_HUMAN] Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. May link the DNA damage surveillance network to the mitotic fidelity checkpoint. Negatively influences the G1/S cell cycle progression without interfering with centrosome duplication. Binds DNA. May be involved in the regulation of PRC2 and PRC3 complex-dependent gene silencing.[1]

About this Structure

4l7p is a 1 chain structure. Full crystallographic information is available from OCA.

Reference

  • Lindgren AE, Karlberg T, Ekblad T, Spjut S, Thorsell AG, Andersson CD, Nhan TT, Hellsten V, Weigelt J, Linusson A, Schuler H, Elofsson M. Chemical probes to study ADP-ribosylation: synthesis and biochemical evaluation of inhibitors of the human ADP-ribosyltransferase ARTD3/PARP3. J Med Chem. 2013 Dec 12;56(23):9556-68. doi: 10.1021/jm401394u. Epub 2013 Nov 22. PMID:24188023 doi:http://dx.doi.org/10.1021/jm401394u
  1. ↑ Rouleau M, McDonald D, Gagne P, Ouellet ME, Droit A, Hunter JM, Dutertre S, Prigent C, Hendzel MJ, Poirier GG. PARP-3 associates with polycomb group bodies and with components of the DNA damage repair machinery. J Cell Biochem. 2007 Feb 1;100(2):385-401. PMID:16924674 doi:10.1002/jcb.21051

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OCA

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