Browse our latest Structural Biology and Molecular Biophysics articles

The crystal structure of a mammalian protein kinase G reveals contacts between the regulatory and catalytic domains, indicates how cGMP binding alters domain conformations and thus domain:domain interactions, and informs a model for enzyme auto-inhibition and cooperative activation.

Structural and biochemical analysis of semisynthetic Akt forms and mutants has revealed the importance of a key interaction network involving Arg86, Glu17, and Tyr18 that controls Akt conformation and activity.

Deleting the first helix of the α-catenin actin-binding domain results in a slip bond interaction between the cadherin–catenin complex and F-actin, such that the binding interaction is stable at low force.

The coupling of the enzyme/structure core to different short linear motifs represents a novel mechanism to diversify and expand the function of signaling proteins.

SmartScope is the first software package designed to streamline, standardize, and fully automate screening of specimens in cryo-electron microscopy, providing real-time remote control of the microscope and access to data through a standard web interface.

Reconstructed ancestral muscle-type acetylcholine receptor β-subunits readily form homopentameric ion channels that open spontaneously, and display functional hallmarks of the modern-day heteropentameric receptor despite being devoid of canonical agonist-binding sites.

In vitro single-particle tracking reveals that ATP binding increases the one-dimensional diffusion of yeast chromatin remodeler SWR1 on DNA stretched between optical tweezers and diffusion is confined by protein roadblocks and nucleosomes.

Single-particle cryo-EM structures reveal a multistep process of how DNA is loaded into the DNA sliding clamp proliferating cell nuclear antigen by the canonical clamp loader replication factor C.

The damage of the bacterial cell envelope is found to be only a secondary effect of the antimicrobial activity of lactoferricin derivatives.

The sour receptor, OTOP1, and related proton channel OTOP3 are steeply activated by extracellular protons while OTOP2 is active over a broad pH range and differences in gating are partly attributed to extracellular domains.