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Construction of a binding site for human immunodeficiency virus type 1 gp120 in rat CD4
The human immunodeficiency virus (HIV-1) infects T lymphocytes via an interaction between the virus envelope glycoprotein gp120 and the CD4 antigen of T helper cells. Previous studies demonstrated that mutations in various regions of CD4 domain 1 lead to the loss of gp120 binding. In the present stu...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1992
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119094/ https://www.ncbi.nlm.nih.gov/pubmed/1730924 |
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collection | PubMed |
description | The human immunodeficiency virus (HIV-1) infects T lymphocytes via an interaction between the virus envelope glycoprotein gp120 and the CD4 antigen of T helper cells. Previous studies demonstrated that mutations in various regions of CD4 domain 1 lead to the loss of gp120 binding. In the present study the gp120 binding site was constructed in rat CD4 by replacing rat with human CD4 sequence. A series of mutants was constructed the best of which bound gp120 with an affinity only twofold less than that of human CD4. The data indicate that the gp120 binding site of human CD4 is constituted by residues 33-58 of domain 1. |
format | Text |
id | pubmed-2119094 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1992 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21190942008-04-16 Construction of a binding site for human immunodeficiency virus type 1 gp120 in rat CD4 J Exp Med Articles The human immunodeficiency virus (HIV-1) infects T lymphocytes via an interaction between the virus envelope glycoprotein gp120 and the CD4 antigen of T helper cells. Previous studies demonstrated that mutations in various regions of CD4 domain 1 lead to the loss of gp120 binding. In the present study the gp120 binding site was constructed in rat CD4 by replacing rat with human CD4 sequence. A series of mutants was constructed the best of which bound gp120 with an affinity only twofold less than that of human CD4. The data indicate that the gp120 binding site of human CD4 is constituted by residues 33-58 of domain 1. The Rockefeller University Press 1992-01-01 /pmc/articles/PMC2119094/ /pubmed/1730924 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles Construction of a binding site for human immunodeficiency virus type 1 gp120 in rat CD4 |
title | Construction of a binding site for human immunodeficiency virus type 1 gp120 in rat CD4 |
title_full | Construction of a binding site for human immunodeficiency virus type 1 gp120 in rat CD4 |
title_fullStr | Construction of a binding site for human immunodeficiency virus type 1 gp120 in rat CD4 |
title_full_unstemmed | Construction of a binding site for human immunodeficiency virus type 1 gp120 in rat CD4 |
title_short | Construction of a binding site for human immunodeficiency virus type 1 gp120 in rat CD4 |
title_sort | construction of a binding site for human immunodeficiency virus type 1 gp120 in rat cd4 |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119094/ https://www.ncbi.nlm.nih.gov/pubmed/1730924 |