Mechanisms of cyclin-dependent kinase regulation: Structures of Cdks, their cyclin activators, and Cip and INK4 inhibitors Journal Article
| Author: | Pavletich, N. P. |
| Article Title: | Mechanisms of cyclin-dependent kinase regulation: Structures of Cdks, their cyclin activators, and Cip and INK4 inhibitors |
| Abstract: | The cyclin-dependent kinases (Cdks) have a central role in coordinating the eukaryotic cell division cycle, and also serve to integrate diverse growth-regulatory signals. Cdks are controlled through several different processes involving the binding of activating cyclin subunits, of inhibitory Cip or INK4 subunits, and phosphorylation. Crystallographic studies of Cdks in four different complexes, reviewed here, have revealed the mechanisms by which these regulatory processes control the Cdk switches. All of these mechanisms involve conformational changes in and around the catalytic cleft of the kinase, indicating that Cdks have evolved an intrinsic conformational flexibility. This flexibility is central to their ability to switch states in response to a diverse range of growth-regulatory signals. |
| Keywords: | review; protein conformation; animals; enzyme activation; phosphorylation; enzyme phosphorylation; enzyme regulation; enzyme inhibitors; models, molecular; conformational transition; cyclin-dependent kinase inhibitor p16; cyclin-dependent kinase inhibitor p21; cycline; cyclin-dependent kinases; cyclins; cyclin dependent kinase; cyclin dependent kinase inhibitor; enzyme structure; enzyme conformation; crystallography; conformational changes; humans; priority journal; cdk-inhibitors |
| Journal Title: | Journal of Molecular Biology |
| Volume: | 287 |
| Issue: | 5 |
| ISSN: | 0022-2836 |
| Publisher: | Academic Press Inc., Elsevier Science |
| Date Published: | 1999-05-16 |
| Start Page: | 821 |
| End Page: | 828 |
| Language: | English |
| DOI: | 10.1006/jmbi.1999.2640 |
| PUBMED: | 10222191 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Review -- Export Date: 16 August 2016 -- Source: Scopus |
