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HIV-1 Intasomes Assembled with Excess Integrase C-Terminal Domain Protein Facilitate Structural Stud...

HIV-1 Intasomes Assembled with Excess Integrase C-Terminal Domain Protein Facilitate Structural Stud...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_bd239db9f5854bfb82b8b6dff9ffb6e8

HIV-1 Intasomes Assembled with Excess Integrase C-Terminal Domain Protein Facilitate Structural Studies by Cryo-EM and Reveal the Role of the Integrase C-Terminal Tail in HIV-1 Integration

About this item

Full title

HIV-1 Intasomes Assembled with Excess Integrase C-Terminal Domain Protein Facilitate Structural Studies by Cryo-EM and Reveal the Role of the Integrase C-Terminal Tail in HIV-1 Integration

Publisher

Switzerland: MDPI AG

Journal title

Viruses, 2024-07, Vol.16 (7), p.1166

Language

English

Formats

Publication information

Publisher

Switzerland: MDPI AG

More information

Scope and Contents

Contents

Retroviral integration is mediated by intasome nucleoprotein complexes wherein a pair of viral DNA ends are bridged together by a multimer of integrase (IN). Atomic-resolution structures of HIV-1 intasomes provide detailed insights into the mechanism of integration and inhibition by clinical IN inhibitors. However, previously described HIV-1 intaso...

Alternative Titles

Full title

HIV-1 Intasomes Assembled with Excess Integrase C-Terminal Domain Protein Facilitate Structural Studies by Cryo-EM and Reveal the Role of the Integrase C-Terminal Tail in HIV-1 Integration

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_bd239db9f5854bfb82b8b6dff9ffb6e8

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_bd239db9f5854bfb82b8b6dff9ffb6e8

Other Identifiers

ISSN

1999-4915

E-ISSN

1999-4915

DOI

10.3390/v16071166

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