Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

L368F/V408F double mutant of IBD of LEDGF/p75 retains interaction with M178I mutant of HIV-1 integrase.

Biochemical and biophysical research communications - 19 Aug 2017

George Anu, Raghavendra Nidhanapati K

Abstract excerpt

Lens-epithelium-derived-growth factor (LEDGF/p75) is an essential host protein for integration of HIV-1 DNA into host genome. Earlier alanine scanning mutational analysis has revealed that residues I365, D366 and F406 in the integrase binding domain (IBD) of p75 are critical for interaction with HIV-1 integrase (IN), while K364, V408 have intermediate effect and residues N367, L368, R405, K407 show wild type...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to HIV Integrase
Share to Intercellular Signaling Peptides and Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Protein Binding

Share to Protein Domains

Source

Identifiers

PMID: 28610923
DOI: 10.1016/j.bbrc.2017.06.035

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

L368F/V408F double mutant of IBD of LEDGF/p75 retains interaction with M178I mutant of HIV-1 integrase.PMID 28610923Read ↗

Blocking the interaction between HIV-1 integrase and human LEDGF/p75: mutational studies, virtual screening and molecular dynamics simulations.Semantic proximity Read ↗

Implication of serine residues 271, 273, and 275 in the human immunodeficiency virus type 1 cofactor activity of lens epithelium-derived growth factor/p75.Semantic proximity Read ↗

Virus evolution reveals an exclusive role for LEDGF/p75 in chromosomal tethering of HIV.Semantic proximity Read ↗

A novel co-crystal structure affords the design of gain-of-function lentiviral integrase mutants in the presence of modified PSIP1/LEDGF/p75.Semantic proximity Read ↗

Overexpression of the Lens Epithelium-Derived Growth Factor/p75 Integrase Binding Domain Inhibits Human Immunodeficiency Virus ReplicationSemantic proximity Read ↗

Structural basis for the recognition between HIV-1 integrase and transcriptional coactivator p75Semantic proximity Read ↗

Inhibitors of the Interactions between HIV‐1 IN and the Cofactor LEDGF/p75Semantic proximity Read ↗

Identification of an Evolutionarily Conserved Domain in Human Lens Epithelium-derived Growth Factor/Transcriptional Co-activator p75 (LEDGF/p75) That Binds HIV-1 IntegraseSemantic proximity Read ↗

The LEDGF/p75 integrase interaction, a novel target for anti-HIV therapySemantic proximity Read ↗

Structure-based virtual screening toward the discovery of novel inhibitors for impeding the protein-protein interaction between HIV-1 integrase and human lens epithelium-derived growth factor (LEDGF/p75)Semantic proximity Read ↗

Lens Epithelium-derived Growth Factor/p75 Interacts with the Transposase-derived DDE Domain of PogZSemantic proximity Read ↗

Inhibitory profile of a LEDGF/p75 peptide against HIV-1 integrase: insight into integrase-DNA complex formation and catalysis.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.