Identification of a novel ATPase activity in 14-3-3 proteins--evidence from enzyme kinetics, structure guided modeling and mutagenesis studies.

14-3-3 Proteins bind phosphorylated sequences in proteins and regulate multiple cellular functions. For the first time, we show that pure recombinant human 14-3-3 ζ, γ, ε and τ isofoms hydrolyze ATP with similar Km and kcat values. In sharp contrast the sigma isoform has no detectable activity.

Rationalizing protein-ligand interactions for PTP1B inhibitors using computational methods.

Protein tyrosine phosphatase 1B inhibitors were reported to have anti-diabetic properties and hence this enzyme has become interesting drug target in the recent time. Huge amount of data is available in public domain about the PTP1B inhibitors in the form of X-ray structures. This study is an attempt to transform this data into useful knowledge which can be directly used to design more effective protein tyrosine phosphatase inhibitors.