Browse our latest Structural Biology and Molecular Biophysics articles

Components of the nuclear pore complex share structural and functional features with soluble nuclear transport receptors, which suggests that there may be an evolutionary relationship between these two types of protein.

Cryo-electron microscopy has been used to provide a structural interpretation of the complete action cycle of release factor 3 during translation termination, which includes a coordinated sequence of interactions with a class-I release factor and the ribosome.

Charybdotoxin, a toxin produced by scorpions, blocks a K⁺ channel by binding in a lock-and-key fashion to the mouth of the channel and presenting a lysine amino group, which serves as a K⁺ mimic in the selectivity filter.

Experiments on synthetic models of synaptic vesicles have shed new light on the role of the protein α-synuclein in the central nervous system.

The details of how the enzyme DNA polymerase α initiates the polymerization of nucleotides in DNA replication, a critical step in the synthesis of new chromosomal DNA, have been revealed in atomic detail.

Electron cryo-microscopy has been used to determine the structure of Chikungunya virus-like particles and to provide new insights into their interactions with four different antibodies.

The structure of a large hydrogenase complex involved in the production of methane by microbes has been determined with cryo-electron microscopy.

Structure-function analysis of the super elongation complex formed when HIV replicates inside cells reveals that the HIV-1 Tat protein binds to a cleft between P-TEFb, an enzyme that is involved in normal transcription, and AFF4, a protein that is used to build the super elongation complex