Ontology highlight
ABSTRACT:
SUBMITTER: Sluchanko NN
PROVIDER: S-EPMC5321513 | biostudies-literature | 2017 Feb
REPOSITORIES: biostudies-literature
Sluchanko Nikolai N NN Beelen Steven S Kulikova Alexandra A AA Weeks Stephen D SD Antson Alfred A AA Gusev Nikolai B NB Strelkov Sergei V SV
Structure (London, England : 1993) 20170112 2
By interacting with hundreds of protein partners, 14-3-3 proteins coordinate vital cellular processes. Phosphorylation of the small heat shock protein, HSPB6, within its intrinsically disordered N-terminal domain activates its interaction with 14-3-3, ultimately triggering smooth muscle relaxation. After analyzing the binding of an HSPB6-derived phosphopeptide to 14-3-3 using isothermal calorimetry and X-ray crystallography, we have determined the crystal structure of the complete assembly consi ...[more]