David W. Borhani

TL;DR: An atomic-level description of the binding process suggests opportunities for allosteric modulation and provides a structural foundation for future optimization of drug–receptor binding and unbinding rates.

TL;DR: A mechanistic model for the sodium/potassium/calcium voltage-gated ion channel superfamily is proposed that reconciles apparently conflicting experimental data.

TL;DR: An activation mechanism for the β2-adrenergic receptor, a prototypical GPCR, is proposed based on atomic-level simulations in which an agonist-bound receptor transitions spontaneously from the active to the inactive crystallographically observed conformation.

TL;DR: A model for the structure of apo A-I bound to high density lipoprotein is proposed, which consists almost entirely of a pseudo-continuous, amphipathic alpha-helix that is punctuated by kinks at regularly spaced proline residues.

TL;DR: Simulations revealed mechanisms that contribute to positive and negative allosteric modulation of classical ligand binding, including coupled conformational changes of the two binding sites and electrostatic interactions between ligands in these sites, which provide a structural basis for the rational design of allosterics modulators targeting muscarinic and possibly other GPCRs.