Browse our latest Structural Biology and Molecular Biophysics articles

Protein disaggregases employ two mechanically-linked ATPase rings that are under steric control by a wrapped-around coiled-coil belt.

Interactions with Sm proteins can provide a way in which regulatory factors can modulate alternative splice site choices.

Two acidic membrane lipids increase synaptotagmin-1 dwell time and penetration into the membrane, reducing the membrane dissociation of synaptotagmin-1.

Cryo-EM structure of the mammalian respiratory supercomplex containing complexes I, III and IV shows a functional asymmetry of complex III, providing strong evidence for directed electron flow in the respirasome.

Structural and binding studies provide insight into the molecular mechanism of protocadherin-19-mediated adhesion and into the biochemical basis of neurodevelopmental disease.

Extensive benchmarking reveals that errors made when manually building models into near-atomic-resolution cryoEM density may automatically be corrected using an improved Rosetta-based structure refinement method.

Single-molecule resolution of cAMP binding to the ligand binding domain of pacemaking channels in zero-mode waveguides reveals the dynamics of the distinct steps underlying both binding and isomerization of the binding domain.

Detailed structural analysis of NPAS1-ARNT and NPAS3-ARNT complexes, and further comparisons with other bHLH-PAS protein structures, show that this family of mammalian transcription factors have distinct ligand-binding pockets within their molecular architectures.

Crystal structures of γ-protocadherin cell-cell recognition dimers reveal the determinants of clustered protocadherin homophilic specificity and cis interaction region structures alongside mutagenesis data identify the putative cis interface.

Point mutations in a ubiquitous human ATPase called p97/VCP deregulate inter-domain communication, resulting in impaired binding of an adaptor that recruits p97 to endosomal pathways and leading to a degenerative disease of bone, muscle and neurons.