Structural and functional characterization of an unanticipated mode of allosteric activity regulation in ribonucleotide reductases controlled by an ATP-cone in the radical-generating subunit.

Internal dynamics play a crucial functional role in MarR (multiple antibiotic resistance repressor) proteins and their role reconciles the distinct allosteric mechanisms proposed previously.

Atomistic simulations reveal how lipids can allosterically modulate membrane receptors.

The signaling ligand (p)ppGpp regulates the enzyme HPRT across species by binding to a novel class of conserved motif, yet its specificity is allosterically altered through evolution of enzyme oligomerization.

Substrate and effector bound structures of a bacterial ribonucleotide reductase reveal the molecular basis by which substrate preference is modulated by a distal site on the enzyme.

Specific residues within an enzyme integrate allosteric inputs that originate from distinct ligand-binding pockets.

Assembly of the human enzyme inosine monophosphate dehydrogenase 2 into filaments promotes substrate-dependent resistance to feedback inhibition by downstream products, promoting increased flux during proliferative states.

Understanding the complex auto-regulatory mechanisms for guanine nucleotide exchange factors is critically important for fully appreciating the layers of control for small GTPases.

The molecular chaperone BIP from the endoplasmic reticulum is fine-tuned postranslationally through the thermodynamic and kinetic alterations in its conformational ensemble of functionally and structurally distinct physiological forms.

Using a short peptide to regulate the activity of HCN ion channels illustrates how physiological modulators could inspire new drugs. .