Open Access
International Journal of Molecular Sciences, volume 23, issue 6, pages 2908
Complex of HIV-1 Integrase with Cellular Ku Protein: Interaction Interface and Search for Inhibitors
Ilgova Ekaterina
1
,
Galkin Simon
1, 2
,
Khrenova Maria G.
1, 3
,
Gottikh Marina
1, 4
,
Anisenko Andrey
1, 2, 4
Publication type: Journal Article
Publication date: 2022-03-08
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 5.6
ISSN: 16616596, 14220067
PubMed ID:
35328329
Catalysis
Organic Chemistry
Inorganic Chemistry
Physical and Theoretical Chemistry
Computer Science Applications
Spectroscopy
Molecular Biology
General Medicine
Abstract
The interaction of HIV-1 integrase and the cellular Ku70 protein is necessary for HIV replication due to its positive effect on post-integration DNA repair. We have previously described in detail the Ku70 binding site within integrase. However, the integrase binding site in Ku70 remained poorly characterized. Here, using a peptide fishing assay and site-directed mutagenesis, we have identified residues I72, S73, and I76 of Ku70 as key for integrase binding. The molecular dynamics studies have revealed a possible way for IN to bind to Ku70, which is consistent with experimental data. According to this model, residues I72 and I76 of Ku70 form a “leucine zipper” with integrase residues, and, therefore, their concealment by low-molecular-weight compounds should impede the Ku70 interaction with integrase. We have identified such compounds by molecular docking and have confirmed their capacity to inhibit the formation of the integrase complex with Ku70. Our data demonstrate that the site of IN binding within Ku70 identified in the present work may be used for further search for inhibitors of the integrase binding to Ku70.
Citations by journals
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1
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3
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International Journal of Molecular Sciences
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International Journal of Molecular Sciences
3 publications, 75%
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Disease Markers
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Disease Markers
1 publication, 25%
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1
2
3
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Citations by publishers
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1
2
3
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Multidisciplinary Digital Publishing Institute (MDPI)
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Multidisciplinary Digital Publishing Institute (MDPI)
3 publications, 75%
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Hindawi Limited
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Hindawi Limited
1 publication, 25%
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1
2
3
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- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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Ilgova E. et al. Complex of HIV-1 Integrase with Cellular Ku Protein: Interaction Interface and Search for Inhibitors // International Journal of Molecular Sciences. 2022. Vol. 23. No. 6. p. 2908.
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Ilgova E., Galkin S., Khrenova M. G., Serebryakova M. V., Gottikh M., Anisenko A. Complex of HIV-1 Integrase with Cellular Ku Protein: Interaction Interface and Search for Inhibitors // International Journal of Molecular Sciences. 2022. Vol. 23. No. 6. p. 2908.
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TY - JOUR
DO - 10.3390/ijms23062908
UR - https://doi.org/10.3390%2Fijms23062908
TI - Complex of HIV-1 Integrase with Cellular Ku Protein: Interaction Interface and Search for Inhibitors
T2 - International Journal of Molecular Sciences
AU - Ilgova, Ekaterina
AU - Gottikh, Marina
AU - Galkin, Simon
AU - Khrenova, Maria G.
AU - Serebryakova, M. V.
AU - Anisenko, Andrey
PY - 2022
DA - 2022/03/08 00:00:00
PB - Multidisciplinary Digital Publishing Institute (MDPI)
SP - 2908
IS - 6
VL - 23
PMID - 35328329
SN - 1661-6596
SN - 1422-0067
ER -
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@article{2022_Ilgova,
author = {Ekaterina Ilgova and Marina Gottikh and Simon Galkin and Maria G. Khrenova and M. V. Serebryakova and Andrey Anisenko},
title = {Complex of HIV-1 Integrase with Cellular Ku Protein: Interaction Interface and Search for Inhibitors},
journal = {International Journal of Molecular Sciences},
year = {2022},
volume = {23},
publisher = {Multidisciplinary Digital Publishing Institute (MDPI)},
month = {mar},
url = {https://doi.org/10.3390%2Fijms23062908},
number = {6},
pages = {2908},
doi = {10.3390/ijms23062908}
}
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MLA
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Ilgova, Ekaterina, et al. “Complex of HIV-1 Integrase with Cellular Ku Protein: Interaction Interface and Search for Inhibitors.” International Journal of Molecular Sciences, vol. 23, no. 6, Mar. 2022, p. 2908. https://doi.org/10.3390%2Fijms23062908.