@article{
 title = {Structural analysis of viral infectivity factor of HIV type 1 and its interaction with A3G, EloC and EloB},
 type = {article},
 year = {2014},
 identifiers = {[object Object]},
 pages = {e89116},
 volume = {9},
 month = {1},
 publisher = {Public Library of Science},
 editors = {[object Object]},
 id = {42f80a98-4ecc-3a68-9c7f-050ee2a55405},
 created = {2018-02-25T14:01:45.365Z},
 file_attached = {false},
 profile_id = {2821d159-c74d-37fb-9bf7-4f15079b738a},
 last_modified = {2019-06-30T14:45:55.009Z},
 read = {false},
 starred = {false},
 authored = {true},
 confirmed = {true},
 hidden = {false},
 folder_uuids = {a5ede3c7-5289-4cae-a7fe-f009a7d98c07,9b49dbe7-67af-4d25-b6c2-b9aaaead4aa6},
 private_publication = {false},
 abstract = {BACKGROUND: The virion infectivity factor (Vif) is an accessory protein, which is essential for HIV replication in host cells. Vif neutralizes the antiviral host protein APOBEC3 through recruitment of the E3 ubiquitin ligase complex.\n\nMETHODOLOGY: Fifty thousand Vif models were generated using the ab initio relax protocol of the Rosetta algorithm from sets of three- and nine-residue fragments using the fragment Monte Carlo insertion-simulated annealing strategy, which favors protein-like features, followed by an all-atom refinement. In the protocol, a constraints archive was used to define the spatial relationship between the side chains from Cys/His residues and zinc ions that formed the zinc-finger motif that is essential for Vif function. We also performed centroids analysis and structural analysis with respect to the formation of the zinc-finger, and the residue disposal in the protein binding domains. Additionally, molecular docking was used to explore details of Vif-A3G and Vif-EloBC interactions. Furthermore, molecular dynamics simulation was used to evaluate the stability of the complexes Vif-EloBC-A3G and Vif-EloC.\n\nPRINCIPAL FINDINGS: The zinc in the HCCH domain significantly alters the folding of Vif and changes the structural dynamics of the HCCH region. Ab initio modeling indicated that the Vif zinc-finger possibly displays tetrahedral geometry as suggested by Mehle et al. (2006). Our model also showed that the residues L146 and L149 of the BC-box motif bind to EloC by hydrophobic interactions, and the residue P162 of the PPLP motif is important to EloB binding.\n\nCONCLUSIONS/SIGNIFICANCE: The model presented here is the first complete three-dimensional structure of the Vif. The interaction of Vif with the A3G protein and the EloBC complex is in agreement with empirical data that is currently available in the literature and could therefore provide valuable structural information for advances in rational drug design.},
 bibtype = {article},
 author = {Da Costa, Kauê Santana and Leal, Elcio and Dos Santos, Alberto Monteiro and Lima E Lima, Anderson Henrique and Alves, Cláudio Nahum and Lameira, Jerônimo},
 journal = {PLoS ONE},
 number = {2}
}

{"_id":"J4utkNzoxx4xkNxLo","bibbaseid":"dacosta-leal-dossantos-limaelima-alves-lameira-structuralanalysisofviralinfectivityfactorofhivtype1anditsinteractionwitha3gelocandelob-2014","authorIDs":["5d2637594aa3adee0100016b"],"author_short":["Da Costa, K., S.","Leal, E.","Dos Santos, A., M.","Lima E Lima, A., H.","Alves, C., N.","Lameira, J."],"bibdata":{"title":"Structural analysis of viral infectivity factor of HIV type 1 and its interaction with A3G, EloC and EloB","type":"article","year":"2014","identifiers":"[object Object]","pages":"e89116","volume":"9","month":"1","publisher":"Public Library of Science","editors":"[object Object]","id":"42f80a98-4ecc-3a68-9c7f-050ee2a55405","created":"2018-02-25T14:01:45.365Z","file_attached":false,"profile_id":"2821d159-c74d-37fb-9bf7-4f15079b738a","last_modified":"2019-06-30T14:45:55.009Z","read":false,"starred":false,"authored":"true","confirmed":"true","hidden":false,"folder_uuids":"a5ede3c7-5289-4cae-a7fe-f009a7d98c07,9b49dbe7-67af-4d25-b6c2-b9aaaead4aa6","private_publication":false,"abstract":"BACKGROUND: The virion infectivity factor (Vif) is an accessory protein, which is essential for HIV replication in host cells. Vif neutralizes the antiviral host protein APOBEC3 through recruitment of the E3 ubiquitin ligase complex.\\n\\nMETHODOLOGY: Fifty thousand Vif models were generated using the ab initio relax protocol of the Rosetta algorithm from sets of three- and nine-residue fragments using the fragment Monte Carlo insertion-simulated annealing strategy, which favors protein-like features, followed by an all-atom refinement. In the protocol, a constraints archive was used to define the spatial relationship between the side chains from Cys/His residues and zinc ions that formed the zinc-finger motif that is essential for Vif function. We also performed centroids analysis and structural analysis with respect to the formation of the zinc-finger, and the residue disposal in the protein binding domains. Additionally, molecular docking was used to explore details of Vif-A3G and Vif-EloBC interactions. Furthermore, molecular dynamics simulation was used to evaluate the stability of the complexes Vif-EloBC-A3G and Vif-EloC.\\n\\nPRINCIPAL FINDINGS: The zinc in the HCCH domain significantly alters the folding of Vif and changes the structural dynamics of the HCCH region. Ab initio modeling indicated that the Vif zinc-finger possibly displays tetrahedral geometry as suggested by Mehle et al. (2006). Our model also showed that the residues L146 and L149 of the BC-box motif bind to EloC by hydrophobic interactions, and the residue P162 of the PPLP motif is important to EloB binding.\\n\\nCONCLUSIONS/SIGNIFICANCE: The model presented here is the first complete three-dimensional structure of the Vif. The interaction of Vif with the A3G protein and the EloBC complex is in agreement with empirical data that is currently available in the literature and could therefore provide valuable structural information for advances in rational drug design.","bibtype":"article","author":"Da Costa, Kauê Santana and Leal, Elcio and Dos Santos, Alberto Monteiro and Lima E Lima, Anderson Henrique and Alves, Cláudio Nahum and Lameira, Jerônimo","journal":"PLoS ONE","number":"2","bibtex":"@article{\n title = {Structural analysis of viral infectivity factor of HIV type 1 and its interaction with A3G, EloC and EloB},\n type = {article},\n year = {2014},\n identifiers = {[object Object]},\n pages = {e89116},\n volume = {9},\n month = {1},\n publisher = {Public Library of Science},\n editors = {[object Object]},\n id = {42f80a98-4ecc-3a68-9c7f-050ee2a55405},\n created = {2018-02-25T14:01:45.365Z},\n file_attached = {false},\n profile_id = {2821d159-c74d-37fb-9bf7-4f15079b738a},\n last_modified = {2019-06-30T14:45:55.009Z},\n read = {false},\n starred = {false},\n authored = {true},\n confirmed = {true},\n hidden = {false},\n folder_uuids = {a5ede3c7-5289-4cae-a7fe-f009a7d98c07,9b49dbe7-67af-4d25-b6c2-b9aaaead4aa6},\n private_publication = {false},\n abstract = {BACKGROUND: The virion infectivity factor (Vif) is an accessory protein, which is essential for HIV replication in host cells. Vif neutralizes the antiviral host protein APOBEC3 through recruitment of the E3 ubiquitin ligase complex.\\n\\nMETHODOLOGY: Fifty thousand Vif models were generated using the ab initio relax protocol of the Rosetta algorithm from sets of three- and nine-residue fragments using the fragment Monte Carlo insertion-simulated annealing strategy, which favors protein-like features, followed by an all-atom refinement. In the protocol, a constraints archive was used to define the spatial relationship between the side chains from Cys/His residues and zinc ions that formed the zinc-finger motif that is essential for Vif function. We also performed centroids analysis and structural analysis with respect to the formation of the zinc-finger, and the residue disposal in the protein binding domains. Additionally, molecular docking was used to explore details of Vif-A3G and Vif-EloBC interactions. Furthermore, molecular dynamics simulation was used to evaluate the stability of the complexes Vif-EloBC-A3G and Vif-EloC.\\n\\nPRINCIPAL FINDINGS: The zinc in the HCCH domain significantly alters the folding of Vif and changes the structural dynamics of the HCCH region. Ab initio modeling indicated that the Vif zinc-finger possibly displays tetrahedral geometry as suggested by Mehle et al. (2006). Our model also showed that the residues L146 and L149 of the BC-box motif bind to EloC by hydrophobic interactions, and the residue P162 of the PPLP motif is important to EloB binding.\\n\\nCONCLUSIONS/SIGNIFICANCE: The model presented here is the first complete three-dimensional structure of the Vif. The interaction of Vif with the A3G protein and the EloBC complex is in agreement with empirical data that is currently available in the literature and could therefore provide valuable structural information for advances in rational drug design.},\n bibtype = {article},\n author = {Da Costa, Kauê Santana and Leal, Elcio and Dos Santos, Alberto Monteiro and Lima E Lima, Anderson Henrique and Alves, Cláudio Nahum and Lameira, Jerônimo},\n journal = {PLoS ONE},\n number = {2}\n}","author_short":["Da Costa, K., S.","Leal, E.","Dos Santos, A., M.","Lima E Lima, A., H.","Alves, C., N.","Lameira, J."],"bibbaseid":"dacosta-leal-dossantos-limaelima-alves-lameira-structuralanalysisofviralinfectivityfactorofhivtype1anditsinteractionwitha3gelocandelob-2014","role":"author","urls":{},"downloads":0,"html":""},"bibtype":"article","creationDate":"2019-07-10T19:07:05.277Z","downloads":0,"keywords":[],"search_terms":["structural","analysis","viral","infectivity","factor","hiv","type","interaction","a3g","eloc","elob","da costa","leal","dos santos","lima e lima","alves","lameira"],"title":"Structural analysis of viral infectivity factor of HIV type 1 and its interaction with A3G, EloC and EloB","year":2014}