title: Bridging the gap between SCF and ubiquitin transfer.
abstract: The first crystal structure of a core SCF complex has been determined to 3.2 A. Together with previous data obtained for RING E3-E2 and Skp1-Skp2 adaptor complexes, the structure provides substantial insight into SCF-mediated protein modification by ubiquitin, a process that regulates protein modification and degradation in systems ranging from cell cycle progression to transcription.
authors.affiliation: Weill Medical College of Cornell University, Department of Biochemistry, Structural Biology Program, 1300 York Avenue, New York, NY 10021, USA.
authors.forename: Christopher D
authors.initials: CD
authors.lastname: Lima
mesh_terms: D001665:Binding Sites; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D010453:Peptide Synthases / Q000378:metabolism*; D044843:SKP Cullin F-Box Protein Ligases; D013379:Substrate Specificity; D025801:Ubiquitin / Q000378:metabolism*
chemical_list: D025801:Ubiquitin; D044843:SKP Cullin F-Box Protein Ligases; D010453:Peptide Synthases