Open and closed conformations of the isolated transmembrane domain of death receptor 5 support a new model of activation.
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ABSTRACT:
SUBMITTER: Lewis AK
PROVIDER: S-EPMC3984993 | biostudies-literature | 2014 Mar
REPOSITORIES: biostudies-literature
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Open and closed conformations of the isolated transmembrane domain of death receptor 5 support a new model of activation.
Lewis Andrew K AK James Zachary M ZM McCaffrey Jesse E JE Braun Anthony R AR Karim Christine B CB Thomas David D DD Sachs Jonathan N JN
Biophysical journal 20140301 6
It has long been presumed that activation of the apoptosis-initiating Death Receptor 5, as well as other structurally homologous members of the TNF-receptor superfamily, relies on ligand-stabilized trimerization of noninteracting receptor monomers. We and others have proposed an alternate model in which the TNF-receptor dimer-sitting at the vertices of a large supramolecular receptor network of ligand-bound receptor trimers-undergoes a closed-to-open transition, propagated through a scissorslike ...[more]
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