Simulation of different truncated p16(INK4a) forms and in silico study of interaction with Cdk4.

ABSTRACT: Protein-protein interactions studies can greatly increase the amount of structural and functional information pertaining to biologically active molecules and processes. The information obtained from such studies can lead to design and application of new modification in order to obtain a desired bioactivity. Many application packages and servers performing docking, such as HEX, DOT, AUTODOCK, and ZDOCK are now available for predicting the lowest free energy state of a protein complex. In this study, we have focused on cyclin-dependent kinase 4 (Cdk4), a key molecule in the regulation of cell cycle progression at the G(1)-S phase restriction point and p16(INK4a), a tumor suppressor which inhibits Cdk4 activity. Truncated structures were created to find the more critical regions of p16 for in

SUBMITTER: Fahham N 

PROVIDER: S-EPMC2664699 | biostudies-literature | 2009

REPOSITORIES: biostudies-literature