4epp: Difference between revisions
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==Canonical poly(ADP-ribose) glycohydrolase from Tetrahymena thermophila.== | ==Canonical poly(ADP-ribose) glycohydrolase from Tetrahymena thermophila.== | ||
<StructureSection load='4epp' size='340' side='right' caption='[[4epp]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='4epp' size='340' side='right'caption='[[4epp]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4epp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Tetth Tetth]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EPP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EPP FirstGlance]. <br> | <table><tr><td colspan='2'>[[4epp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Tetth Tetth]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EPP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EPP FirstGlance]. <br> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Tetth]] | [[Category: Tetth]] | ||
[[Category: Dunstan, M S]] | [[Category: Dunstan, M S]] | ||
Revision as of 10:58, 27 March 2019
Canonical poly(ADP-ribose) glycohydrolase from Tetrahymena thermophila.Canonical poly(ADP-ribose) glycohydrolase from Tetrahymena thermophila.
Structural highlights
Publication Abstract from PubMedPoly(ADP-ribosyl)ation is a reversible post-translational protein modification involved in the regulation of a number of cellular processes including DNA repair, chromatin structure, mitosis, transcription, checkpoint activation, apoptosis and asexual development. The reversion of poly(ADP-ribosyl)ation is catalysed by poly(ADP-ribose) (PAR) glycohydrolase (PARG), which specifically targets the unique PAR (1-2') ribose-ribose bonds. Here we report the structure and mechanism of the first canonical PARG from the protozoan Tetrahymena thermophila. In addition, we reveal the structure of T. thermophila PARG in a complex with a novel rhodanine-containing mammalian PARG inhibitor RBPI-3. Our data demonstrate that the protozoan PARG represents a good model for human PARG and is therefore likely to prove useful in guiding structure-based discovery of new classes of PARG inhibitors. Structure and mechanism of a canonical poly(ADP-ribose) glycohydrolase.,Dunstan MS, Barkauskaite E, Lafite P, Knezevic CE, Brassington A, Ahel M, Hergenrother PJ, Leys D, Ahel I Nat Commun. 2012 Jun 6;3:878. doi: 10.1038/ncomms1889. PMID:22673905[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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