A computational study of the phosphorylation mechanism of the insulin receptor tyrosine kinase.

ABSTRACT: Although various groups have studied the phosphorylation mechanism of the insulin receptor tyrosine kinase (IRK), an unanimous picture has not yet emerged. In this work, we performed a computational study to gain further insights. We first built a structural model of the reactant complex with the guide of several crystal structures and previous computational studies of the cyclic AMP-dependent protein kinase. We then optimized the structure by performing geometry optimization using a quantum mechanical model containing nearly 300 atoms. A reaction path was then traced between the reactant and the product by using a multiple coordinate-driven method. The calculations mapped out a sequence of structural changes depicting the conversion of the reactant to the product. Analysis of the structur

SUBMITTER: Zhou B 

PROVIDER: S-EPMC2785087 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature