{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Bacot-Davis VR"],"funding":["NCRR NIH HHS","NIAID NIH HHS","NIGMS NIH HHS"],"pagination":["15792-7"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4226078"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["111(44)"],"pubmed_abstract":["Cardiovirus Leader (L) proteins induce potent antihost inhibition of active cellular nucleocytoplasmic trafficking by triggering aberrant hyperphosphorylation of nuclear pore proteins (Nup). To achieve this, L binds protein RanGTPase (Ran), a key trafficking regulator, and diverts it into tertiary or quaternary complexes with required kinases. The activity of L is regulated by two phosphorylation events not required for Ran binding. Matched NMR studies on the unphosphorylated, singly, and doubly phosphorylated variants of Mengovirus L (L(M)) show both modifications act together to partially stabilize a short internal α-helix comprising L(M) residues 43-46. This motif implies that ionic and Van der Waals forces contributed by phosphorylation help organize downstream residues 48-67 into a ne"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase."],"pmcid":["PMC4226078"],"funding_grant_id":["P41GM66326","S10RR025062","P41 GM066326","R56 AI017331","S10 RR023438","S10RR029220","T32 AI078985","T32 GM007215","P41 RR002301","S10 RR029220","S10RR023438","S10 RR025062","S10 RR008438","S10 RR002781","R01 AI017331","P41RR02301"],"pubmed_authors":["Ciomperlik JJ","Cornilescu CC","Palmenberg AC","Bacot-Davis VR","Basta HA"],"additional_accession":[]},"is_claimable":false,"name":"Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase.","description":"Cardiovirus Leader (L) proteins induce potent antihost inhibition of active cellular nucleocytoplasmic trafficking by triggering aberrant hyperphosphorylation of nuclear pore proteins (Nup). To achieve this, L binds protein RanGTPase (Ran), a key trafficking regulator, and diverts it into tertiary or quaternary complexes with required kinases. The activity of L is regulated by two phosphorylation events not required for Ran binding. Matched NMR studies on the unphosphorylated, singly, and doubly phosphorylated variants of Mengovirus L (L(M)) show both modifications act together to partially stabilize a short internal α-helix comprising L(M) residues 43-46. This motif implies that ionic and Van der Waals forces contributed by phosphorylation help organize downstream residues 48-67 into a ne","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Nov","modification":"2026-05-03T22:37:25.897Z","creation":"2019-03-27T01:39:14Z"},"accession":"S-EPMC4226078","cross_references":{"pubmed":["25331866"],"doi":["10.1073/pnas.1411098111"]}}