3uel

Crystal structure of the catalytic domain of rat poly (ADP-ribose) glycohydrolase bound to ADP-HPDCrystal structure of the catalytic domain of rat poly (ADP-ribose) glycohydrolase bound to ADP-HPD

Structural highlights 3uel is a 3 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PARG_RAT Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. PARG acts both as an endo- and exoglycosidase, releasing PAR of different length as well as ADP-ribose monomers. Required for retinoid acid-dependent gene transactivation, probably by dePARsylating histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters (By similarity). See Also Poly(ADP-ribose) glycohydrolase 3D structures

spinqualitylabelsall models 3uel, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image