title: Compact Parkin only: insights into the structure of an autoinhibited ubiquitin ligase.
abstract: Mutations in Parkin represent ~50% of disease-causing defects in autosomal recessive-juvenile onset Parkinson's disease (AR-JP). Recently, there have been four structural reports of autoinhibited forms of this RING-IBR-RING (RBR) ubiquitin ligase (E3) by the Gehring, Komander, Johnston and Shaw groups. The important advances from these studies set the stage for the next steps in understanding the molecular basis for Parkinson's disease (PD).
authors.affiliation: Structural Biophysics Laboratory, Center for Cancer Research National Cancer Institute, Frederick, MD, USA. byrdra@mail.nih.gov
authors.forename: R Andrew
authors.initials: RA
authors.lastname: Byrd
authors.forename: Allan M
authors.initials: AM
authors.lastname: Weissman
mesh_terms: D000818:Animals; D006801:Humans; D009154:Mutation; D020734:Parkinsonian Disorders / Q000201:enzymology / Q000235:genetics; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship; D044767:Ubiquitin-Protein Ligases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: D044767:Ubiquitin-Protein Ligases; C111567:parkin protein