The mechanism of H171T resistance reveals the importance of Nδ-protonated His171 for the binding of...
The mechanism of H171T resistance reveals the importance of Nδ-protonated His171 for the binding of allosteric inhibitor BI-D to HIV-1 integrase
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Publisher
England: BioMed Central
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Language
English
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Publisher
England: BioMed Central
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Contents
Allosteric HIV-1 integrase (IN) inhibitors (ALLINIs) are an important new class of anti-HIV-1 agents. ALLINIs bind at the IN catalytic core domain (CCD) dimer interface occupying the principal binding pocket of its cellular cofactor LEDGF/p75. Consequently, ALLINIs inhibit HIV-1 IN interaction with LEDGF/p75 as well as promote aberrant IN multimeri...
Alternative Titles
Full title
The mechanism of H171T resistance reveals the importance of Nδ-protonated His171 for the binding of allosteric inhibitor BI-D to HIV-1 integrase
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TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4251946
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4251946
Other Identifiers
ISSN
1742-4690
E-ISSN
1742-4690
DOI
10.1186/s12977-014-0100-1
