The butyrophilin 3A1 intracellular domain undergoes a conformational change involving the juxtamembrane region.

ABSTRACT: Small isoprenoid diphosphates, such as (E)-4-hydroxy-3-methyl-but-2-enyl diphosphate (HMBPP), are ligands of the internal domain of BTN3A1. Ligand binding in target cells promotes activation of Vγ9Vδ2 T cells. We demonstrate by small-angle X-ray scattering (SAXS) that HMBPP binding to the internal domain of BTN3A1 induces a conformational change in the position of the B30.2 domain relative to the juxtamembrane (JM) region. To better understand the molecular details of this conformational rearrangement, NMR spectroscopy was used to discover that the JM region interacts with HMBPP, specifically at the diphosphate. The spectral location of the affected amide peaks, partial NMR assignments, and JM mutants (ST²⁹⁶AA or T³⁰⁴A) investigated, confirm that the backbone a

SUBMITTER: Nguyen K 

PROVIDER: S-EPMC5636706 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature