TRIM5α SPRY/coiled-coil interactions optimize avid retroviral capsid recognition.

ABSTRACT: Restriction factors are important components of intrinsic cellular defense mechanisms against viral pathogens. TRIM5α is a restriction factor that intercepts the incoming capsid cores of retroviruses such as HIV and provides an effective species-specific barrier to retroviral infection. The TRIM5α SPRY domain directly binds the capsid with only very weak, millimolar-level affinity, and productive capsid recognition therefore requires both TRIM5α dimerization and assembly of the dimers into a multivalent hexagonal lattice to promote avid binding. Here, we explore the important unresolved question of whether the SPRY domains are flexibly linked to the TRIM lattice or more precisely positioned to maximize avidity. Biochemical and biophysical experiments indicate that the linker segment connec

SUBMITTER: Roganowicz MD 

PROVIDER: S-EPMC5667893 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature