Ruthenium half-sandwich complexes bound to protein kinase Pim-1.
|Author||Debreczeni, Judit E; Bullock, Alex N; Atilla, G Ekin; et al|
|Subject||Crystallography, X-Ray Models, Molecular Protein Kinase Inhibitors Protein Structure, Tertiary Proto-Oncogene Proteins c-pim-1 Ruthenium Stereoisomerism chemistry chemistry metabolism chemistry metabolism|
Crystal Structures of the p21-activated kinases PAK4, PAK5, and PAK6 reveal catalytic domain plasticity of active group II PAKs.
|Abstract||p21-activated kinases have been classified into two groups based on their domain architecture. Group II PAKs (PAK4-6) regulate a wide variety of cellular functions, and PAK deregulation has been linked to tumor development. Structural comparison of five high-resolution structures comprising all active, monophosphorylated group II catalytic domains revealed a surprising degree of domain plasticity, including a number of catalytically productive an ... [truncated at 450 characters in length]|
|Author||Eswaran, Jeyanthy; Lee, Wen Hwa; Debreczeni, Judit E; et al|
|Subject||Amino Acid Sequence Animals Catalytic Domain Crystallography Molecular Sequence Data Protein Conformation Protein Kinase Inhibitors Protein-Serine-Threonine Kinases Purines drug effects genetics chemistry pharmacology antagonists and inhibitors chemistry genetics chemistry|
Insights into protein kinase regulation and inhibition by large scale structural comparison.
|Abstract||Protein structure determination of soluble globular protein domains has developed into an efficient routine technology which can now be applied to generate and analyze structures of entire human protein families. In the kinase area, several kinase families still lack comprehensive structural analysis. Nevertheless, Structural Genomics (SG) efforts contributed more than 40 kinase catalytic domain structures during the past 4 years providing a rich ... [truncated at 450 characters in length]|
|Author||Eswaran, Jeyanthy; Knapp, Stefan;|
|Subject||Animals Humans Protein Kinase Inhibitors Protein Kinases Protein Structure, Tertiary Structure-Activity Relationship chemistry chemistry genetics metabolism|
Small-molecule kinase inhibitors provide insight into Mps1 cell cycle function.
|Abstract||Mps1, a dual-specificity kinase, is required for the proper functioning of the spindle assembly checkpoint and for the maintenance of chromosomal stability. As Mps1 function has been implicated in numerous phases of the cell cycle, the development of a potent, selective small-molecule inhibitor of Mps1 should facilitate dissection of Mps1-related biology. We describe the cellular effects and Mps1 cocrystal structures of new, selective small-molec ... [truncated at 450 characters in length]|
|Author||Kwiatkowski, Nicholas; Jelluma, Nannette; Filippakopoulos, Panagis; et al|
|Subject||Cell Cycle Cell Cycle Proteins Enzyme Inhibitors Models, Molecular Protein Kinase Inhibitors Protein-Serine-Threonine Kinases physiology pharmacology chemistry pharmacology physiology|
Structural comparison of human mammalian ste20-like kinases.
|Abstract||The serine/threonine mammalian Ste-20 like kinases (MSTs) are key regulators of apoptosis, cellular proliferation as well as polarization. Deregulation of MSTs has been associated with disease progression in prostate and colorectal cancer. The four human MSTs are regulated differently by C-terminal regions flanking the catalytic domains.|
|Author||Record, Christopher J; Chaikuad, Apirat; Rellos, Peter; et al|
|Subject||Adenosine Triphosphate Amino Acid Sequence Binding Sites Biomimetic Materials Crystallography, X-Ray Enzyme Activation Humans Models, Molecular Molecular Sequence Data Phosphorylation Protein Conformation Protein Kinase Inhibitors Protein Multimerization Protein-Serine-Threonine Kinases Quinazolines Sequence Homology, Amino Acid Substrate Specificity metabolism chemistry metabolism pharmacology chemistry metabolism pharmacology antagonists and inhibitors chemistry metabolism chemistry metabolism pharmacology|