Poly (ADP-ribose) glycohydrolase
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
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. | 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. | ||
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| + | == 3D Structures of poly (ADP-ribose) glycohydrolase == | ||
| + | [[Poly(ADP-ribose) glycohydrolase 3D structures]] | ||
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</StructureSection> | </StructureSection> | ||
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{{#tree:id=OrganizedByTopic|openlevels=0| | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
| - | *Poly (ADP-ribose) glycohydrolase | + | *Poly (ADP-ribose) glycohydrolase;Domains: Arh3 19-363; catalytic 448-976 |
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| + | **[[4a0d]], [[4b1g]] – hPARG catalytic domain (mutant) - human<br /> | ||
| + | **[[5zqy]] – hPARG Arh3 residues 19-363 <br /> | ||
| - | **[[3sih]] – TcPARG – ''Thermonospora curvata''<br /> | ||
| - | **[[3sij]] – TcPARG (mutant) <br /> | ||
**[[3uek]] – rPARG catalytic domain - rat<br /> | **[[3uek]] – rPARG catalytic domain - rat<br /> | ||
**[[4fc2]] – mPARG catalytic domain - mouse<br /> | **[[4fc2]] – mPARG catalytic domain - mouse<br /> | ||
**[[4n9y]], [[4n9z]], [[4na5]], [[4na6]] – mPARG catalytic domain (mutant) <br /> | **[[4n9y]], [[4n9z]], [[4na5]], [[4na6]] – mPARG catalytic domain (mutant) <br /> | ||
**[[2qty]] – mPARG 3 <br /> | **[[2qty]] – mPARG 3 <br /> | ||
| - | **[[ | + | **[[3sih]] – TcPARG – ''Thermonospora curvata''<br /> |
| - | **[[ | + | **[[3sij]] – TcPARG (mutant) <br /> |
| + | **[[5zda]] – DrPARG – ''Deinococcus radiodurans''<br /> | ||
*Poly (ADP-ribose) glycohydrolase complex with ADP-ribose | *Poly (ADP-ribose) glycohydrolase complex with ADP-ribose | ||
| - | **[[3sig]] – TcPARG + ADP-ribose <br /> | ||
| - | **[[4epp]] – TtPARG + ADP-ribose - ''Tetrahymena thermophila'' <br /> | ||
| - | **[[4l2h]], [[5a7r]] – TtPARG (mutant) + ADP-ribose <br /> | ||
**[[4b1h]] – hPARG catalytic domain (mutant) + ADP-ribose<br /> | **[[4b1h]] – hPARG catalytic domain (mutant) + ADP-ribose<br /> | ||
**[[6d36]] – hPARG Arh3 residues 1-363 + ADP-ribose<br /> | **[[6d36]] – hPARG Arh3 residues 1-363 + ADP-ribose<br /> | ||
**[[6d3a]] – hPARG Arh3 residues 1-363 (mutant) + ADP-ribose<br /> | **[[6d3a]] – hPARG Arh3 residues 1-363 (mutant) + ADP-ribose<br /> | ||
**[[4na0]] – mPARG catalytic domain + ADP-ribose<br /> | **[[4na0]] – mPARG catalytic domain + ADP-ribose<br /> | ||
| + | **[[3sig]] – TcPARG + ADP-ribose <br /> | ||
| + | **[[4epp]] – TtPARG + ADP-ribose - ''Tetrahymena thermophila'' <br /> | ||
| + | **[[4l2h]], [[5a7r]] – TtPARG (mutant) + ADP-ribose <br /> | ||
| + | **[[5zdb]], [[5zdc]], [[5zdd]], [[5zde]] – DrPARG + ADP-ribose <br /> | ||
| + | **[[5zdf]] – DrPARG (mutant) + ADP-ribose <br /> | ||
* Poly (ADP-ribose) glycohydrolase complex with inhibitor | * Poly (ADP-ribose) glycohydrolase complex with inhibitor | ||
| - | **[[ | + | **[[4b1i]], [[4b1j]], [[5lhb]], [[6hmk]], [[6hml]], [[6hmm]], [[6hmn]] – hPARG catalytic domain (mutant) + inhibitor<br /> |
**[[3uel]] – rPARG catalytic domain + inhibitor <br /> | **[[3uel]] – rPARG catalytic domain + inhibitor <br /> | ||
| - | **[[4epq]] – TtPARG + inhibitor <br /> | ||
| - | **[[4b1i]], [[4b1j]], [[5lhb]] – hPARG catalytic domain (mutant) + inhibitor<br /> | ||
**[[4na4]] – mPARG catalytic domain + inhibitor <br /> | **[[4na4]] – mPARG catalytic domain + inhibitor <br /> | ||
| + | **[[3sii]] – TcPARG + inhibitor <br /> | ||
| + | **[[4epq]] – TtPARG + inhibitor <br /> | ||
| + | |||
}} | }} | ||
Revision as of 08:07, 25 November 2019
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3D Structures of poly (ADP-ribose) glycohydrolase
Updated on 25-November-2019
References
- ↑ 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
- ↑ Virag L, Szabo C. The therapeutic potential of poly(ADP-ribose) polymerase inhibitors. Pharmacol Rev. 2002 Sep;54(3):375-429. PMID:12223530
- ↑ 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
