Ontology highlight
ABSTRACT:
SUBMITTER: Laughlin JD
PROVIDER: S-EPMC3589125 | biostudies-literature | 2012 Dec
REPOSITORIES: biostudies-literature
Laughlin John D JD Nwachukwu Jerome C JC Figuera-Losada Mariana M Cherry Lisa L Nettles Kendall W KW LoGrasso Philip V PV
Structure (London, England : 1993) 20121108 12
c-Jun N-terminal (JNK) family kinases have a common peptide-docking site used by upstream activating kinases, substrates, scaffold proteins, and phosphatases, where the ensemble of bound proteins determines signaling output. Although there are many JNK structures, little is known about mechanisms of allosteric regulation between the catalytic and peptide-binding sites, and the activation loop, whose phosphorylation is required for catalytic activity. Here, we compare three structures of unligand ...[more]