title: Cyclin-dependent kinases: inhibition and substrate recognition.
abstract: Four unresolved issues of cyclin-dependent kinase (CDK) regulation have been addressed by structural studies this year - the mechanism of CDK inhibition by members of the INK4 family of CDK inhibitors, consensus substrate sequence recognition by CDKs, the role of the cyclin subunit in substrate recognition and the structural mechanism underlying CDK inhibition by phosphorylation.
authors.affiliation: Laboratory of Molecular Biophysics, Department of Biochemistry, Oxford Centre for Molecular Sciences, Oxford, OX1 3QU, UK. Jane@biop.ox.ac.uk
authors.forename: J A
authors.initials: JA
authors.lastname: Endicott
authors.forename: M E
authors.initials: ME
authors.lastname: Noble
authors.forename: J A
authors.initials: JA
authors.lastname: Tucker
mesh_terms: D001665:Binding Sites; D018797:Cell Cycle Proteins / Q000378:metabolism; D018844:Cyclin-Dependent Kinases / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism*; D016213:Cyclins / Q000378:metabolism; D008958:Models, Molecular; D015394:Molecular Structure; D010766:Phosphorylation; D013379:Substrate Specificity
chemical_list: D018797:Cell Cycle Proteins; D016213:Cyclins; D018844:Cyclin-Dependent Kinases