Thermal unfolding of the archaeal DNA and RNA binding protein Ssh10.
|Abstract||The reversible thermal unfolding of the archaeal histone-like protein Ssh10b from the extremophile Sulfolobus shibatae was studied using differential scanning calorimetry and circular dichroism spectroscopy. Analytical ultracentrifugation and gel filtration showed that Ssh10b is a stable dimer in the pH range 2.5-7.0. Thermal denaturation data fit into a two-state unfolding model, suggesting that the Ssh10 dimer unfolds as a single cooperative un ... [truncated at 450 characters in length]|
|Author||Wu, Xiaoqiu; Oppermann, Madalina; Berndt, Kurt D; et al|
Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation.
|Abstract||The SH2 domain of cytoplasmic tyrosine kinases can enhance catalytic activity and substrate recognition, but the molecular mechanisms by which this is achieved are poorly understood. We have solved the structure of the prototypic SH2-kinase unit of the human Fes tyrosine kinase, which appears specialized for positive signaling. In its active conformation, the SH2 domain tightly interacts with the kinase N-terminal lobe and positions the kinase al ... [truncated at 450 characters in length]|
|Author||Filippakopoulos, Panagis; Kofler, Michael; Hantschel, Oliver; et al|