High-resolution structure of the Influenza A virus PB2cap binding domain illuminates the changes induced by ligand binding

In this report, the anatomic behavior of the influenza A virus PB2cap domain is established by solving the crystal structure of native influenza A virus PB2cap at 1.52   Å resolution. By comparing it with the ligand-bound structure, the dissociation and rotation of the ligand-binding domain in PB2cap from the C-terminal domain is identified. This domain movement is present in many PB2cap structures, suggesting its functional relevance for polymerase activity.

Source: Acta Crystallographica Section F - February 26, 2018 Category: Biochemistry Authors: Constantinides, A. Gumpper, R. Severin, C. Luo, M. Tags: high resolution structures transcription polymerase basic protein 2 RNA polymerase cap-snatching domain movement Influenza A virus research communications Source Type: research