Poly (ADP-ribose) glycohydrolase

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<StructureSection load='3sig' size='340' side='right' caption='Structure of human poly (ADP-ribose) glycohydrolase catalytic domain complex with ADP-ribose (stick model) (PDB code [[3sig]]). ' scene=''>
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<StructureSection load='' size='350' side='right' caption='Structure of human poly (ADP-ribose) glycohydrolase catalytic domain complex with ADP-ribose (PDB code [[3sig]]). ' scene='59/595759/Cv/1'>
== Function ==
== Function ==
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'''Poly (ADP-ribose) glycohydrolase''' (PARG) hydrolizes the ribose-ribose bonds in poly (ADP-ribose). Poly (ADP-ribose) are synthesized after DNA damage. PARG acts as both endo- and exoglycosidase and releases poly (ADP-ribose) of different lengths including monomers.
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'''Poly (ADP-ribose) glycohydrolase''' (PARG) hydrolizes the ribose-ribose bonds in poly (ADP-ribose). Poly (ADP-ribose) are synthesized after DNA damage. PARG acts as both endo- and exoglycosidase and releases poly (ADP-ribose) of different lengths including monomers<ref>PMID:11376691</ref>.
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== Disease ==
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== Relevance ==
== Relevance ==
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PARG deficiency leads to cell death.
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PARG deficiency leads to cell death. Over-activation of PARP due to oxidative stress culminates in cell dysfunction and necrosis. PARP inhibitors have anti-inflammatory effect<ref>PMID:12223530</ref>.
== Structural highlights ==
== Structural highlights ==
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The <scene name='59/595759/Cv/4'>active site</scene> of PARG contains <scene name='59/595759/Cv/5'>two catalytic glutamic acid residues</scene><ref>PMID:21892188</ref>. Water molecules are shown as red spheres.
== 3D Structures of poly (ADP-ribose) glycohydrolase ==
== 3D Structures of poly (ADP-ribose) glycohydrolase ==
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[[Poly(ADP-ribose) glycohydrolase 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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===PARG ===
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[[3sih]] – TcPARG – ''Thermonospora curvata''<br />
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[[3sij]] – TcPARG (mutant) <br />
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[[3uek]] – rPARG catalytic domain - rat<br />
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[[4fc2]] – mPARG catalytic domain - mouse<br />
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[[4n9y]], [[4n9z]], [[4na5]], [[4na6]] – mPARG catalytic domain (mutant) <br />
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[[4a0d]], [[4b1g]] – hPARG catalytic domain (mutant) - human<br />
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===PARG complex with ADP-ribose===
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[[3sig]] – TcPARG + ADP-ribose <br />
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[[4epp]] – TtPARG + ADP-ribose - ''Tetrahymena thermophila'' <br />
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[[4l2h]] – TtPARG (mutant) + ADP-ribose <br />
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[[4b1h]] – hPARG catalytic domain (mutant) + ADP-ribose<br />
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[[4na0]] – mPARG catalytic domain + ADP-ribose<br />
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===PARG complex with inhibitor===
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[[3sii]] – TcPARG + inhibitor <br />
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[[3uel]] – rPARG catalytic domain + inhibitor <br />
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[[4epq]] – TtPARG + inhibitor <br />
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[[4b1i]], [[4b1j]] – hPARG catalytic domain (mutant) + inhibitor<br />
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[[4na4]] – mPARG catalytic domain + inhibitor <br />
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== References ==
== References ==

Current revision

Structure of human poly (ADP-ribose) glycohydrolase catalytic domain complex with ADP-ribose (PDB code 3sig).

Drag the structure with the mouse to rotate

References

  1. ↑ Herceg Z, Wang ZQ. Functions of poly(ADP-ribose) polymerase (PARP) in DNA repair, genomic integrity and cell death. Mutat Res. 2001 Jun 2;477(1-2):97-110. PMID:11376691
  2. ↑ Virag L, Szabo C. The therapeutic potential of poly(ADP-ribose) polymerase inhibitors. Pharmacol Rev. 2002 Sep;54(3):375-429. PMID:12223530
  3. ↑ Slade D, Dunstan MS, Barkauskaite E, Weston R, Lafite P, Dixon N, Ahel M, Leys D, Ahel I. The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase. Nature. 2011 Sep 4. doi: 10.1038/nature10404. PMID:21892188 doi:10.1038/nature10404

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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