Defining residues involved in human rhinovirus 2A proteinase substrate recognition
作者： Carla Sousa , Eva M. Schmid , Tim Skern
DOI: 10.1016/J.FEBSLET.2006.09.023
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摘要: Abstract The 2A proteinase (2Apro) of human rhinoviruses (HRVs) initiates proteolytic processing by cleaving between the C-terminus VP1 and its own N-terminus. It subsequently cleaves host protein eIF4GI. HRV2 HRV14 2Apro cleave at IITTA ∗ GPSD DIKSY ∗ GLGP on their respective polyproteins. cleavage site eIF4GI is TLSTR ∗ GPPR. We show that can self-process sequence whereas cannot, due to presence arginine residue P1. mutations A104C or A104S in restored when was present P1, although not wild-type levels. These experiments define residues which determine substrate recognition rhinoviral 2Apro.
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