Conformational states dynamically populated by a kinase determine its function
نویسندگان
چکیده
منابع مشابه
Probing Conformational Feature of a Recombinant Pyruvate Kinase by Limited Proteolysis
Pyruvate kinase is a key enzyme in glycolytic pathway that catalyzes the transphosphorylation between phosphoenolpyruvate and ADP to yield ATP and Pyruvate. Geobacillus stearothermophillus has a stable pyruvate kinase with determined crystal structure that composed of four separate domains. Given that limited proteolysis experiments can be successfully used to probe conformational features of p...
متن کاملDynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy.
Protein kinase A (PKA) is a ubiquitous phosphoryl transferase that mediates hundreds of cell signaling events. During turnover, its catalytic subunit (PKA-C) interconverts between three major conformational states (open, intermediate, and closed) that are dynamically and allosterically activated by nucleotide binding. We show that the structural transitions between these conformational states a...
متن کاملVesicle Geometries Enabled by Dynamically Trapped States.
Understanding and controlling vesicle shapes is a fundamental challenge in biophysics and materials design. In this paper, we design dynamic protocols for enlarging the shape space of both fluid and crystalline vesicles beyond the equilibrium zone. By removing water from within the vesicle at different rates, we numerically produced a series of dynamically trapped stable vesicle shapes for both...
متن کاملprobing conformational feature of a recombinant pyruvate kinase by limited proteolysis
pyruvate kinase is a key enzyme in glycolytic pathway that catalyzes the transphosphorylation between phosphoenolpyruvate and adp to yield atp and pyruvate. geobacillus stearothermophillus has a stable pyruvate kinase with determined crystal structure that composed of four separate domains. given that limited proteolysis experiments can be successfully used to probe conformational features of p...
متن کاملHsp90 dependence of a kinase is determined by its conformational landscape
Heat shock protein 90 (Hsp90) is an abundant molecular chaperone, involved in the folding and activation of 60% of the human kinome. The oncogenic tyrosine kinase v-Src is one of the most stringent client proteins of Hsp90, whereas its almost identical homolog c-Src is only weakly affected by the chaperone. Here, we perform atomistic molecular simulations and in vitro kinase assays to explore t...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Science
سال: 2020
ISSN: 0036-8075,1095-9203
DOI: 10.1126/science.abc2754