Article

Evolutionary plasticity of SH3 domain binding by Nef proteins of the HIV-1/SIVcpz lentiviral lineage

2021-06-22

Abstract excerpt

<h4>ABSTRACT</h4> The accessory protein Nef of human and simian immunodeficiency viruses (HIV and SIV) is an important pathogenicity factor known to interact with cellular protein kinases and other signaling proteins. A canonical SH3 domain binding motif in Nef is required for most of these interactions. For example, HIV-1 Nef activates the tyrosine kinase Hck by tightly binding to its SH3 domain. An archetypal c...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 03adc23c-4355-5924-b97e-dd88f2d1849d
DOI: 10.1101/2021.06.22.449400

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Evolutionary plasticity of SH3 domain binding by Nef proteins of the HIV-1/SIVcpz lentiviral lineageDOI 10.1101/2021.06.22.449400Read

Synergy and allostery in ligand binding by HIV-1 NefSemantic proximity Read

Conformation of the Dileucine‐Based Sorting Motif in HIV‐1 Nef Revealed by Intermolecular Domain AssemblySemantic proximity Read

Crystal Structure of the Conserved Core of HIV-1 Nef Complexed with a Src Family SH3 DomainSemantic proximity Read

The Nef protein of primate lentivirusesSemantic proximity Read

Endocytic sorting motif interactions involved in Nef-mediated downmodulation of CD4 and CD3.Semantic proximity Read

Overlapping effector interfaces define the multiple functions of the HIV-1 Nef polyproline helix.Semantic proximity Read

The Binding Interface between Human APOBEC3F and HIV-1 Vif Elucidated by Genetic and Computational ApproachesSemantic proximity Read

Structural perspectives on HIV‐1 Vif and APOBEC3 restriction factor interactionsSemantic proximity Read

Conserved residues in the HIV-1 Nef hydrophobic pocket are essential for recruitment and activation of the Hck tyrosine kinase.Semantic proximity Read

Structural basis of HIV-1 Vif-mediated E3 ligase targeting of host APOBEC3HSemantic proximity Read

Maintenance of AP-2-Dependent Functional Activities of Nef Restricts Pathways of Immune Escape from CD8 T Lymphocyte Responses.Semantic proximity Read

Loop 1 of APOBEC3C regulates its antiviral activity against HIV-1Semantic proximity Read