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Defining Drug Interactions with the Viral Membrane Protein Vpu from HIV-1
The replication of HIV-1 is strongly enhanced by a small membrane protein called virus protein U (Vpu). Vpu achieves its task by (a) interacting with CD4, the HIV-1 receptor, and (b) by amplifying particle release at the site of the plasma membrane. While the first role is due to interactions of the...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2005
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7120575/ http://dx.doi.org/10.1007/0-387-28146-0_14 |
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author | Lemaitre, V. Kim, C. G. Fischer, D. Lam, Y. H. Watts, A. Fischer, W. B. |
author_facet | Lemaitre, V. Kim, C. G. Fischer, D. Lam, Y. H. Watts, A. Fischer, W. B. |
author_sort | Lemaitre, V. |
collection | PubMed |
description | The replication of HIV-1 is strongly enhanced by a small membrane protein called virus protein U (Vpu). Vpu achieves its task by (a) interacting with CD4, the HIV-1 receptor, and (b) by amplifying particle release at the site of the plasma membrane. While the first role is due to interactions of the cytoplasmic site of Vpu with CD4, the second role may be due to ion channel activity caused by the self-assembly of the protein. Recently, a blocker has been proposed which abolishes channel activity. In this chapter, the mechanism of blocking is described using computational methods, including a brief overview of other viral ion channel blockers. |
format | Online Article Text |
id | pubmed-7120575 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2005 |
record_format | MEDLINE/PubMed |
spelling | pubmed-71205752020-04-06 Defining Drug Interactions with the Viral Membrane Protein Vpu from HIV-1 Lemaitre, V. Kim, C. G. Fischer, D. Lam, Y. H. Watts, A. Fischer, W. B. Viral Membrane Proteins: Structure, Function, and Drug Design Article The replication of HIV-1 is strongly enhanced by a small membrane protein called virus protein U (Vpu). Vpu achieves its task by (a) interacting with CD4, the HIV-1 receptor, and (b) by amplifying particle release at the site of the plasma membrane. While the first role is due to interactions of the cytoplasmic site of Vpu with CD4, the second role may be due to ion channel activity caused by the self-assembly of the protein. Recently, a blocker has been proposed which abolishes channel activity. In this chapter, the mechanism of blocking is described using computational methods, including a brief overview of other viral ion channel blockers. 2005 /pmc/articles/PMC7120575/ http://dx.doi.org/10.1007/0-387-28146-0_14 Text en © Kluwer Academic/Plenum Publishers, New York 2005 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic. |
spellingShingle | Article Lemaitre, V. Kim, C. G. Fischer, D. Lam, Y. H. Watts, A. Fischer, W. B. Defining Drug Interactions with the Viral Membrane Protein Vpu from HIV-1 |
title | Defining Drug Interactions with the Viral Membrane Protein Vpu from HIV-1 |
title_full | Defining Drug Interactions with the Viral Membrane Protein Vpu from HIV-1 |
title_fullStr | Defining Drug Interactions with the Viral Membrane Protein Vpu from HIV-1 |
title_full_unstemmed | Defining Drug Interactions with the Viral Membrane Protein Vpu from HIV-1 |
title_short | Defining Drug Interactions with the Viral Membrane Protein Vpu from HIV-1 |
title_sort | defining drug interactions with the viral membrane protein vpu from hiv-1 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7120575/ http://dx.doi.org/10.1007/0-387-28146-0_14 |
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