Allosteric Activation of PI3Kα Results in Dynamic Access to Catalytically Competent Conformations.
Sign Up to like & getrecommendations! Published in 2020 at "Structure"
DOI: 10.1016/j.str.2020.01.010
Abstract: Class I phosphoinositide-3-kinases (PI3Ks) phosphorylate PIP2 at its 3' inositol position to generate PIP3, a second messenger that influences signaling cascades regulating cellular growth, survival, and proliferation. Previous studies have suggested that PI3Kα activation involves… read more here.
Keywords: pi3k; activation pi3k; allosteric activation; nsh2 domain ... See more keywords
The kinetics of folding of the NSH2 domain from p85
Sign Up to like & getrecommendations! Published in 2019 at "Scientific Reports"
DOI: 10.1038/s41598-019-40480-2
Abstract: SH2 domains are protein domains that mediate protein-protein interaction through the recognition and binding of specific sequences containing phosphorylated tyrosines. The p85 protein is the regulatory subunit of the heterodimeric enzyme PI3K, an important enzyme… read more here.
Keywords: folding nsh2; kinetics folding; domain p85; nsh2 domain ... See more keywords