Abstract
Cyclin-dependent kinase 2 (CDK2) is a member of a highly conserved family of protein kinases that regulate the eukaryotic cell cycle. The crystal structures of the human CDK2 apoenzyme and its Mg2+ ATP complex have been determined to 2.4 A resolution. The structure is bi-lobate, like that of the cyclic AMP-dependent protein kinase, but contains a unique helix-loop segment that interferes with ATP and protein substrate binding and probably plays a key part in the regulation of all cyclin-dependent kinases.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, Non-P.H.S.
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Adenosine Triphosphate / chemistry
-
Adenosine Triphosphate / metabolism
-
Amino Acid Sequence
-
Binding Sites
-
CDC2-CDC28 Kinases*
-
Computer Simulation
-
Crystallography
-
Cyclin-Dependent Kinase 2
-
Cyclin-Dependent Kinases*
-
Cyclins / metabolism
-
Humans
-
Models, Molecular
-
Molecular Sequence Data
-
Phosphorylation
-
Protein Conformation
-
Protein Kinases / chemistry*
-
Protein Kinases / metabolism
-
Protein Serine-Threonine Kinases*
Substances
-
Cyclins
-
Adenosine Triphosphate
-
Protein Kinases
-
Protein Serine-Threonine Kinases
-
CDC2-CDC28 Kinases
-
CDK2 protein, human
-
Cyclin-Dependent Kinase 2
-
Cyclin-Dependent Kinases