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L(565)M mutation in HIV-1 glycoprotein 41 stabilizes the coiled-coil structure

N-terminal and C-terminal heptad repeats (NHR and CHR) of HIV type 1 (HIV-1) glycoprotein 41 are known to be regions directly related to cell fusion during virus attack, and their complex core constructs a coiled-coil structure in the fusion process. In our recent studies, MT-4/17-3-6, a strain of H...

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Autores principales: Yamamoto, Daisuke, Li, Gui-Mei, Ikuta, Kazuyoshi, Goto, Toshiyuki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Inc. 2005
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7092850/
https://www.ncbi.nlm.nih.gov/pubmed/16054592
http://dx.doi.org/10.1016/j.bbrc.2005.07.052
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author Yamamoto, Daisuke
Li, Gui-Mei
Ikuta, Kazuyoshi
Goto, Toshiyuki
author_facet Yamamoto, Daisuke
Li, Gui-Mei
Ikuta, Kazuyoshi
Goto, Toshiyuki
author_sort Yamamoto, Daisuke
collection PubMed
description N-terminal and C-terminal heptad repeats (NHR and CHR) of HIV type 1 (HIV-1) glycoprotein 41 are known to be regions directly related to cell fusion during virus attack, and their complex core constructs a coiled-coil structure in the fusion process. In our recent studies, MT-4/17-3-6, a strain of HIV-1, showed the strong resistance to peptide fusion inhibitors compared with other strains such as MT-4/LAI, L-2 and CU98-26, and had a distinctive L(565)M mutation in the central region of NHR. To investigate the relationship between the mutation and resistance, we performed a molecular modeling of the coiled-coil of MT-4/17-3-6 by using energy minimization and molecular dynamics simulation based on the MT-4/LAI X-ray structure. As a result, we found that H(564) in the NHR was pushed to the outer side by this mutation, and three hydrogen bond bridges of Y(638)-H(564)-E(560)-Q(650) could be formed, enclosing the coiled-coil. The binding of peptide inhibitors would be disturbed by the structural stabilization of these bridges in MT-4/17-3-6.
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spelling pubmed-70928502020-03-25 L(565)M mutation in HIV-1 glycoprotein 41 stabilizes the coiled-coil structure Yamamoto, Daisuke Li, Gui-Mei Ikuta, Kazuyoshi Goto, Toshiyuki Biochem Biophys Res Commun Article N-terminal and C-terminal heptad repeats (NHR and CHR) of HIV type 1 (HIV-1) glycoprotein 41 are known to be regions directly related to cell fusion during virus attack, and their complex core constructs a coiled-coil structure in the fusion process. In our recent studies, MT-4/17-3-6, a strain of HIV-1, showed the strong resistance to peptide fusion inhibitors compared with other strains such as MT-4/LAI, L-2 and CU98-26, and had a distinctive L(565)M mutation in the central region of NHR. To investigate the relationship between the mutation and resistance, we performed a molecular modeling of the coiled-coil of MT-4/17-3-6 by using energy minimization and molecular dynamics simulation based on the MT-4/LAI X-ray structure. As a result, we found that H(564) in the NHR was pushed to the outer side by this mutation, and three hydrogen bond bridges of Y(638)-H(564)-E(560)-Q(650) could be formed, enclosing the coiled-coil. The binding of peptide inhibitors would be disturbed by the structural stabilization of these bridges in MT-4/17-3-6. Elsevier Inc. 2005-09-16 2005-07-22 /pmc/articles/PMC7092850/ /pubmed/16054592 http://dx.doi.org/10.1016/j.bbrc.2005.07.052 Text en Copyright © 2005 Elsevier Inc. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Yamamoto, Daisuke
Li, Gui-Mei
Ikuta, Kazuyoshi
Goto, Toshiyuki
L(565)M mutation in HIV-1 glycoprotein 41 stabilizes the coiled-coil structure
title L(565)M mutation in HIV-1 glycoprotein 41 stabilizes the coiled-coil structure
title_full L(565)M mutation in HIV-1 glycoprotein 41 stabilizes the coiled-coil structure
title_fullStr L(565)M mutation in HIV-1 glycoprotein 41 stabilizes the coiled-coil structure
title_full_unstemmed L(565)M mutation in HIV-1 glycoprotein 41 stabilizes the coiled-coil structure
title_short L(565)M mutation in HIV-1 glycoprotein 41 stabilizes the coiled-coil structure
title_sort l(565)m mutation in hiv-1 glycoprotein 41 stabilizes the coiled-coil structure
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7092850/
https://www.ncbi.nlm.nih.gov/pubmed/16054592
http://dx.doi.org/10.1016/j.bbrc.2005.07.052
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