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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...

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Autores principales: Jafari, Elham, Gheysarzadeh, Ali, Mahnam, Karim, Shahmohammadi, Rezvan, Ansari, Amir, Bakhtyari, Hadi, Mofid, Mohammad Reza
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Medknow Publications & Media Pvt Ltd 2018
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.
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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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