Structural and dynamical characterization of SERINC, an integral membrane HIV restriction factor

Abstract

In humans, the family of Serine incorporators (SERINC) are integral membrane proteins which restrict HIV infection by interfering with the virus-cell fusion step of the HIV infection cycle. The relationships between SERINC structure, composed of bundled transmembrane helices, dynamics, and biological function remain poorly understood. Here, full length protein structures for human and Drosophila Melanogaster SERINCs were derived using cryo-EM densities and AlphaFold2. Atomistic models were further refined using MolProbity-score based structural refinement, embedded in atomistic lipid bilayers of varying compositions, and solvated under physiological conditions (150mM NaCl).