Browse our latest Structural Biology and Molecular Biophysics articles

Channel characteristics of the presequence translocation pore have a direct impact on protein import into the mitochondrial matrix.

Small probes show that most AMPA receptors are constrained near or in the synapses.

An atomic model of the 3744-residue Tra1 protein reveals multiple transcription activator binding sites, its integration within the SAGA chromatin coactivator complex, and a striking similarity to DNA-repair factor DNA-PKcs.

A flip of the dimer asymmetry following the first ATP hydrolysis provides a mechanistic model for client remodeling by the mitochondrial Hsp90, TRAP1.

The SHIP2 inositol phosphatase is an important upstream regulator of the Akt signaling pathway, which requires a catalytic core formed by the phosphatase domain tightly packed to a C2 domain for its function.

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.

The structures of photosystem II, with the water-oxidizing Mn4CaO5-cluster fully removed and in an intermediate assembly state, show that photoassembly is facilitated by perfectly pre-arranged protein ligands of the five metal ions.

Agonist and antagonist peptides of the corticotropin-releasing factor receptor type 1 adopt different folds and stabilize distinct conformations of the receptor transmembrane domain, which involves tilting of helices VI and VII around conserved glycine hinges.

Sequence conservation in Ras depends strongly on the biochemical network in which it operates, providing a framework for understanding the origin of global selection pressures on proteins.

Single molecule microscopy combined with biochemical analyses show that a two-step lipid-binding mechanism of the SRP receptor balances the trade-off between speed and specificity during co-translational protein targeting.