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Article

Nucleoporin NUP153 phenylalanine-glycine motifs engage a common binding pocket within the HIV-1 capsid protein to mediate lentiviral infectivity.

PLoS pathogens - 1 Jan 2013

Matreyek Kenneth A, Yücel Sara S, Li Xiang, Engelman Alan

Abstract excerpt

Lentiviruses can infect non-dividing cells, and various cellular transport proteins provide crucial functions for lentiviral nuclear entry and integration. We previously showed that the viral capsid (CA) protein mediated the dependency on cellular nucleoporin (NUP) 153 during HIV-1 infection, and now demonstrate a direct interaction between the CA N-terminal domain and the phenylalanine-glycine (FG)-repeat...

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Share to Active Transport, Cell Nucleus
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to gag Gene Products, Human Immunodeficiency Virus

Share to Hydrophobic and Hydrophilic Interactions

Share to mRNA Cleavage and Polyadenylation Factors

Share to Nuclear Pore Complex Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 24130490
DOI: 10.1371/journal.ppat.1003693
PMCID: PMC3795039

Genes

CPSF6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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