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Stimulation of GMP formation in hGBP1 is mediated by W79 and its effect on the antiviral activity
Author(s) -
Raninga Nikunj,
Nayeem Shahid M.,
Gupta Sowmiya,
Mullick Ranajoy,
Pandita Esha,
Das Saumitra,
Deep Shashank,
Sau Apurba Kumar
Publication year - 2021
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15611
Subject(s) - gtpase , chemistry , conformational change , gtp' , cleavage (geology) , biochemistry , biophysics , mutant , stimulation , microbiology and biotechnology , stereochemistry , biology , enzyme , gene , paleontology , fracture (geology) , neuroscience
The underlying mechanism of assembly‐stimulated GMP formation by large GTPase hGBP1 is not fully clarified. Here, we suggest that after first phosphate cleavage, the W79‐containing region undergoes a conformational change, which helps to reposition the active site for the next cleavage through a stable contact between the W79 side chain and the main chain of K76. We also showed that stimulated GMP formation is crucial for suppression of HCV proliferation.