4l7u: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4l7u|  PDB=4l7u  |  SCENE=  }}
===Human artd3 (parp3) - catalytic domain in complex with inhibitor ME0398===
{{ABSTRACT_PUBMED_24188023}}


The entry 4l7u is ON HOLD until Paper Publication
==Function==
[[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>  


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.
==About this Structure==
[[4l7u]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L7U OCA].  


Description: Human artd3 (parp3) -catalytic domain in complex with inhibitor ME0398
==Reference==
<ref group="xtra">PMID:024188023</ref><references group="xtra"/><references/>
[[Category: Andersson, C D.]]
[[Category: Ekblad, T.]]
[[Category: Elofsson, M.]]
[[Category: Karlberg, T.]]
[[Category: Lindgren, A E.G.]]
[[Category: Linusson, A.]]
[[Category: Schuler, H.]]
[[Category: Spjut, S.]]
[[Category: Thorsell, A G.]]
[[Category: Weigelt, J.]]
[[Category: Adp-ribosylation]]
[[Category: Diphtheria toxin like adp-ribose transferase]]
[[Category: Transferase]]
[[Category: Transferase-transferase inhibitor complex]]

Revision as of 20:23, 19 February 2014

Template:STRUCTURE 4l7u

Human artd3 (parp3) - catalytic domain in complex with inhibitor ME0398Human artd3 (parp3) - catalytic domain in complex with inhibitor ME0398

Template:ABSTRACT PUBMED 24188023

FunctionFunction

[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 StructureAbout this Structure

4l7u is a 1 chain structure. Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. 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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