Abstract:
:An F35L mutation in the N-terminal domain of the polymerase acidic protein (PA-Nter), which contains the active site of the endonuclease, has been reported to result in higher polymerase activity in mouse-adapted strains of the 2009 pandemic influenza A H1N1 virus. We modeled wild and mutant complexes of uridine 5'-monophosphate (UMP) as the endonuclease substrate and performed molecular dynamics simulations. The results demonstrated that the F35L mutation could result in a changed orientation of a helix containing active site residues and improve the ligand affinity in the mutant strain. This study suggests a molecular mechanism of enhanced polymerase activity.
journal_name
Arch Viroljournal_title
Archives of virologyauthors
Bhoye D,Cherian SSdoi
10.1007/s00705-017-3681-xsubject
Has Abstractpub_date
2018-04-01 00:00:00pages
1031-1036issue
4eissn
0304-8608issn
1432-8798pii
10.1007/s00705-017-3681-xjournal_volume
163pub_type
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pub_type: 杂志文章
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journal_title:Archives of virology
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更新日期:2003-09-01 00:00:00
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