The mechanism of H171T resistance reveals the importance of N[delta]-protonated His171 for the bindi...
The mechanism of H171T resistance reveals the importance of N[delta]-protonated His171 for the binding of allosteric inhibitor BI-D to HIV-1 integrase
About this item
Full title
Author / Creator
Publisher
London: BioMed Central Ltd
Journal title
Language
English
Formats
Publication information
Publisher
London: BioMed Central Ltd
Subjects
More information
Scope and Contents
Contents
Background 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 I...
Alternative Titles
Full title
The mechanism of H171T resistance reveals the importance of N[delta]-protonated His171 for the binding of allosteric inhibitor BI-D to HIV-1 integrase
Authors, Artists and Contributors
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_proquest_journals_1629479734
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_1629479734
Other Identifiers
ISSN
1742-4690
E-ISSN
1742-4690
DOI
10.1186/s12977-014-0100-1
