Browse our latest Structural Biology and Molecular Biophysics articles

The development of an integrative computational-experimental approach for identifying small molecules that can disrupt RNA:protein interactions in vitro and in cells led to the identification of several inhibitors of YBX1 in the micromolar range, including a previously approved drug.

SARS coronaviruses encode several mysterious proteins such as Orf3a and, in contrast to what has been claimed, Orf3a is not an ion channel but rather disrupts cellular trafficking by binding to the protein sorting complex known as HOPS.

A high-throughput analysis of several self-cleaving ribozymes reveals the effect of every possible mutation, and every possible pair of mutations, and how patterns in the relative activity data can be mapped to canonical and non-canonical structural elements.

Novel components in the pathway from malignant hyperthermia to diabetes include promotion of a kinase that impedes glycogen synthesis, increased lysis of junctophilin1 and gene regulatory actions by a junctophilin fragment, surprisingly predicted to oppose the effects of elevated calcium.

Structures of human cytoplasmic dynein-1 bound to its regulator LIS1 reveal the interfaces involved in forming the complex and provide a context for disease-linked mutations.

Biochemical and electrophysiological approaches show that the amphetamine derivative ECSI#6 is an uncompetitive inhibitor of the serotonin transporter and thus the first ever characterized ligand of a solute carrier of this type.

Cryo-EM structure and functional analyses show that human iron exporter ferroportin (Fpn) can bind and transport calcium ions and the transport activity is reduced when the concentration of ferrous ions is high.

PIP₂ inhibits the proton-activated chloride (PAC) channel by selectively stabilizing its desensitized state.

Comparision of current and fluorescent kinetics from P2X7 receptor mutants labeled with the fluorescent amino acid ANAP suggests that the characteristic P2X7 current facilitation involves changes in channel gating rather than interactions or conformational changes of its intracellular ballast domain.

New cryoEM structures reveal how small bacteriophage proteins suppress bacterial immunity.