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In silico interaction of insulin-like growth factor binding protein 3 with insulin-like growth factor 1
Insulin-like growth factor binding protein-3 (IGFBP-3) is a vital protein exist in circulation which interacts with high affinity to insulin-like growth factor (IGFs) altering their activities. Therefore, the interaction between IGFs and IGFBP-3 has a key role altering large spectrum of activities s...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Medknow Publications & Media Pvt Ltd
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6040160/ https://www.ncbi.nlm.nih.gov/pubmed/30065766 http://dx.doi.org/10.4103/1735-5362.235160 |
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author | Jafari, Elham Gheysarzadeh, Ali Mahnam, Karim Shahmohammadi, Rezvan Ansari, Amir Bakhtyari, Hadi Mofid, Mohammad Reza |
author_facet | Jafari, Elham Gheysarzadeh, Ali Mahnam, Karim Shahmohammadi, Rezvan Ansari, Amir Bakhtyari, Hadi Mofid, Mohammad Reza |
author_sort | Jafari, Elham |
collection | PubMed |
description | Insulin-like growth factor binding protein-3 (IGFBP-3) is a vital protein exist in circulation which interacts with high affinity to insulin-like growth factor (IGFs) altering their activities. Therefore, the interaction between IGFs and IGFBP-3 has a key role altering large spectrum of activities such as cell cycle progression, proliferation and apoptosis. Despite decades of research, the crystal structure of IGFBP-3 has not been identified possibly due to some technical challenge in its crystallizing. The three-dimensional (3D) structure of IGFBP-3 was predicted using homology modeling, Phyre2, and molecular dynamic. Its interaction with IGF-1 was also identified by HADDOCK software. IGFBP-3 has the most identity with other IGFBPs in N and C-domain; however, its linker domain has lower identity. Our data predicted that IGF-1 structurally interacts with N-domain and linker domain of IGFBP-3. Some conserved residues of IGFBP-3 such as Glu33, Arg36, Gly39, Arg60, Arg66, Asn109, and Ile146 interacts with Glu3, Asp12, Phe16, Gly19, Asp20, Arg21, and Glu58 of IGF-1. In addition, our data predict that the linker domain has a loop structure which covers post translational modification and interacts with IGF-1. The phosphorylation of Ser111 in linker domain, which previously has been shown to induce apoptosis make a repulsive force interrupting this interaction to IGF-1, which enables IGFBP-3 to induce apoptosis. The present study suggests that the linker domain has a key role in recognition of IGFBP-3 with IGF-1. |
format | Online Article Text |
id | pubmed-6040160 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Medknow Publications & Media Pvt Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-60401602018-08-01 In silico interaction of insulin-like growth factor binding protein 3 with insulin-like growth factor 1 Jafari, Elham Gheysarzadeh, Ali Mahnam, Karim Shahmohammadi, Rezvan Ansari, Amir Bakhtyari, Hadi Mofid, Mohammad Reza Res Pharm Sci Original Article Insulin-like growth factor binding protein-3 (IGFBP-3) is a vital protein exist in circulation which interacts with high affinity to insulin-like growth factor (IGFs) altering their activities. Therefore, the interaction between IGFs and IGFBP-3 has a key role altering large spectrum of activities such as cell cycle progression, proliferation and apoptosis. Despite decades of research, the crystal structure of IGFBP-3 has not been identified possibly due to some technical challenge in its crystallizing. The three-dimensional (3D) structure of IGFBP-3 was predicted using homology modeling, Phyre2, and molecular dynamic. Its interaction with IGF-1 was also identified by HADDOCK software. IGFBP-3 has the most identity with other IGFBPs in N and C-domain; however, its linker domain has lower identity. Our data predicted that IGF-1 structurally interacts with N-domain and linker domain of IGFBP-3. Some conserved residues of IGFBP-3 such as Glu33, Arg36, Gly39, Arg60, Arg66, Asn109, and Ile146 interacts with Glu3, Asp12, Phe16, Gly19, Asp20, Arg21, and Glu58 of IGF-1. In addition, our data predict that the linker domain has a loop structure which covers post translational modification and interacts with IGF-1. The phosphorylation of Ser111 in linker domain, which previously has been shown to induce apoptosis make a repulsive force interrupting this interaction to IGF-1, which enables IGFBP-3 to induce apoptosis. The present study suggests that the linker domain has a key role in recognition of IGFBP-3 with IGF-1. Medknow Publications & Media Pvt Ltd 2018-08 /pmc/articles/PMC6040160/ /pubmed/30065766 http://dx.doi.org/10.4103/1735-5362.235160 Text en Copyright: © 2018 Research in Pharmaceutical Sciences http://creativecommons.org/licenses/by-nc-sa/4.0 This is an open access journal, and articles are distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 4.0 License, which allows others to remix, tweak, and build upon the work non-commercially, as long as appropriate credit is given and the new creations are licensed under the identical terms. |
spellingShingle | Original Article Jafari, Elham Gheysarzadeh, Ali Mahnam, Karim Shahmohammadi, Rezvan Ansari, Amir Bakhtyari, Hadi Mofid, Mohammad Reza In silico interaction of insulin-like growth factor binding protein 3 with insulin-like growth factor 1 |
title | In silico interaction of insulin-like growth factor binding protein 3 with insulin-like growth factor 1 |
title_full | In silico interaction of insulin-like growth factor binding protein 3 with insulin-like growth factor 1 |
title_fullStr | In silico interaction of insulin-like growth factor binding protein 3 with insulin-like growth factor 1 |
title_full_unstemmed | In silico interaction of insulin-like growth factor binding protein 3 with insulin-like growth factor 1 |
title_short | In silico interaction of insulin-like growth factor binding protein 3 with insulin-like growth factor 1 |
title_sort | in silico interaction of insulin-like growth factor binding protein 3 with insulin-like growth factor 1 |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6040160/ https://www.ncbi.nlm.nih.gov/pubmed/30065766 http://dx.doi.org/10.4103/1735-5362.235160 |
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