The number of contacts at the interface of a protein–protein complex, together with the properties of the surface, provides a simple, but well-performing predictor of binding affinity.
Sunbin Liu, Sina Mozaffari-Jovin ... Markus C Wahl
Structural and functional analyses show how the spliceosomal Prp3 protein concomitantly binds double- and single- stranded regions in U4/U6 di-snRNAs and serves to stabilize the U4/U6•U5 tri-snRNP for splicing.
Lys63-linked diubiquitin exists as an ensemble of conformational states, each responsible for binding to a target protein through conformational selection.
Structures of the signal recognition particle before and after it captures a transmembrane domain suggest how it chooses, engages, and shields its clients during membrane protein targeting to the endoplasmic reticulum.
The crystal structure of Norrie Disease Protein in complex with the extracellular cysteine-rich domain of Frizzled4 receptor and sucrose octasulfate reveals binding sites for Frizzled4, low density lipoprotein receptor related protein 5/6, and proteoglycan.
A multidimensional chemical mapping strategy enables confident determination of the structures of non-coding RNAs at 1-nm resolution, including previously intractable riboswitch and human regulon states.
