Приказ основних података о документу
Computational studies of the interaction between the HIV-1 integrase tetramer and the cofactor LEDGF/p75: Insights from molecular dynamics simulations and the informational spectrum method
dc.creator | Tintori, Cristina | |
dc.creator | Veljković, Nevena V. | |
dc.creator | Veljković, Veljko | |
dc.creator | Botta, Maurizio | |
dc.date.accessioned | 2018-03-01T21:29:20Z | |
dc.date.available | 2018-03-01T21:29:20Z | |
dc.date.issued | 2010 | |
dc.identifier.issn | 0887-3585 | |
dc.identifier.uri | https://vinar.vin.bg.ac.rs/handle/123456789/4144 | |
dc.description.abstract | A crystal structure of the integrase binding domain (IBD) of the lens epithelium-derived growth factor (LEDGF/p75) in complex with the dimer of the HIV-1 integrase (IN) catalytic core domain (CCD) provides useful information that might help in the understanding of essential protein-protein contacts in HIV-1. However, mutagenic studies indicated that interactions between the full-length proteins were more extensive than the contacts observed in the co-crystal structure of the isolated domains. On the other hand, the biochemical characterization of the interaction between full-length IN and LEDGF/p75 has recently proved that LEDGF/p75 promotes IN tetramerization with two LEDGF/p75 IBD molecules bound to the IN tetramer. This experimental evidence suggests that to obtain a complete structural description of the interactions between the two proteins, the full-length tetrameric structure of IN should be considered. Our aim was to obtain a detailed picture of HIV-1 IN interactions with cellular co-factors that was of general interest, particularly for the development of small molecule IN inhibitors, which mimic the IBD of LEDGF/p75. To this end, we performed bioinformatics analyses to identify protein sequence domains involved in long-range recognition. Subsequently, we applied molecular dynamics techniques to investigate the detailed interactions between the complete tetrameric form of IN and two molecules of the IBD of LEDGF/p75. Our dynamic picture is in agreement with experimental data and, thereby, provides new details of the IN-LEDGF/p75 interaction. | en |
dc.relation | info:eu-repo/grantAgreement/EC/FP7/242135/EU// | |
dc.relation | Ministero dellIstruzione, dellUniversita e della Ricerca [2008CE75SA_004], MSTD Republic of Serbia [143001] | |
dc.rights | restrictedAccess | en |
dc.source | Proteins: Structure Function and Bioinformatics | en |
dc.subject | hot spots | en |
dc.subject | IN Oligomerization | en |
dc.subject | IN tetramer | en |
dc.subject | protein-protein interactions | en |
dc.title | Computational studies of the interaction between the HIV-1 integrase tetramer and the cofactor LEDGF/p75: Insights from molecular dynamics simulations and the informational spectrum method | en |
dc.type | article | en |
dcterms.abstract | Тинтори, Цристина; Ботта, Мауризио; Вељковић Невена В.; Вељковић Вељко; | |
dc.citation.volume | 78 | |
dc.citation.issue | 16 | |
dc.citation.spage | 3396 | |
dc.citation.epage | 3408 | |
dc.identifier.wos | 000284046400014 | |
dc.identifier.doi | 10.1002/prot.22847 | |
dc.citation.rank | M22 | |
dc.identifier.pmid | 20878714 | |
dc.identifier.scopus | 2-s2.0-78349299377 |
Документи
Датотеке | Величина | Формат | Преглед |
---|---|---|---|
Уз овај запис нема датотека. |