title: Structural biology of the writers, readers, and erasers in mono- and poly(ADP-ribose) mediated signaling.
abstract: ADP-ribosylation of proteins regulates protein activities in various processes including transcription control, chromatin organization, organelle assembly, protein degradation, and DNA repair. Modulating the proteins involved in the metabolism of ADP-ribosylation can have therapeutic benefits in various disease states. Protein crystal structures can help understand the biological functions, facilitate detailed analysis of single residues, as well as provide a basis for development of small molecule effectors. Here we review recent advances in our understanding of the structural biology of the writers, readers, and erasers of ADP-ribosylation.
authors: Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-17177 Stockholm, Sweden.
authors: Tobias
authors: T
authors: Karlberg
authors: Marie-France
authors: MF
authors: Langelier
authors: John M
authors: JM
authors: Pascal
authors: Herwig
authors: H
authors: Schüler
mesh_terms: D036002:ADP Ribose Transferases / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D001419:Bacteria / Q000201:enzymology; D001665:Binding Sites; D004249:DNA Damage; D005786:Gene Expression Regulation; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D011064:Poly Adenosine Diphosphate Ribose / Q000737:chemistry / Q000378:metabolism*; D011065:Poly(ADP-ribose) Polymerases / Q000737:chemistry* / Q000378:metabolism*; D054730:Protein Interaction Domains and Motifs; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D015398:Signal Transduction; D038501:Tankyrases / Q000737:chemistry / Q000378:metabolism
chemical_list: D011064:Poly Adenosine Diphosphate Ribose; D036002:ADP Ribose Transferases; D011065:Poly(ADP-ribose) Polymerases; D038501:Tankyrases; D006026:Glycoside Hydrolases; C022407:poly ADP-ribose glycohydrolase
keywords: ADP-ribosylation; DNA repair; Glycohydrolase; Macro domain; Signaling pathways; Transferase