The C-terminus of A2A receptor drives oligomer formation via an intricate network of disulfide bonds, hydrogen bonds, electrostatic interactions, and hydrophobic interactions, all of which are enhanced by depletion interactions.
Structural analysis of the kinesin-13 MCAK bound to its C-terminal tail reveals the molecular basis for the conformation of kinesin-13 in solution and the mechanism that triggers long-range conformational changes upon microtubule binding.
The structure of a light-sensitive G protein-coupled receptor in complex with a Gi-protein heterotrimer provides a structural foundation for the role of the receptor C-terminal tail in scaffolding and signaling.
A novel region in the CaV2.1 α1 subunit regulates coupling of synaptic vesicles to CaV2.1 calcium channels, synaptic vesicle release and docking, and the size of the fast and total releasable pools of synaptic vesicles.
Highly conserved C-terminal domains of the tumor suppressor BRCA2 are not essential for accumulation at damaged DNA but affect conformation and cell survival, implying roles beyond delivering strand-exchange protein RAD51.
In Escherichia coli structural maintenance of chromosomes (SMC) complex, MukBEF, a dimeric MukF kleisin binds and activates MukB SMC ATPases through two independent interfaces provided by distinct MukF N- and C-terminal domains.
A novel auto-inhibitory mechanism regulates the functional activity of the cellular prion protein, PrPC, providing for the first time a coherent molecular model for both its pathological and physiological effects.