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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doaj-167be93774e24bff92438d86714cb12d2021-07-07T14:29:22ZengWolters Kluwer Medknow PublicationsResearch in Pharmaceutical Sciences1735-53621735-94142018-01-0113433234210.4103/1735-5362.235160In silico interaction of insulin-like growth factor binding protein 3 with insulin-like growth factor 1Elham JafariAli GheysarzadehKarim MahnamRezvan ShahmohammadiAmir AnsariHadi BakhtyariMohammad Reza MofidInsulin-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.http://www.rpsjournal.net/article.asp?issn=1735-5362;year=2018;volume=13;issue=4;spage=332;epage=342;aulast=Jafaridocking study; igf-1; igfbp-3; linker domain; molecular dynamic |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Elham Jafari Ali Gheysarzadeh Karim Mahnam Rezvan Shahmohammadi Amir Ansari Hadi Bakhtyari Mohammad Reza Mofid |
spellingShingle |
Elham Jafari Ali Gheysarzadeh Karim Mahnam Rezvan Shahmohammadi Amir Ansari Hadi Bakhtyari Mohammad Reza Mofid In silico interaction of insulin-like growth factor binding protein 3 with insulin-like growth factor 1 Research in Pharmaceutical Sciences docking study; igf-1; igfbp-3; linker domain; molecular dynamic |
author_facet |
Elham Jafari Ali Gheysarzadeh Karim Mahnam Rezvan Shahmohammadi Amir Ansari Hadi Bakhtyari Mohammad Reza Mofid |
author_sort |
Elham Jafari |
title |
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_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_sort |
in silico interaction of insulin-like growth factor binding protein 3 with insulin-like growth factor 1 |
publisher |
Wolters Kluwer Medknow Publications |
series |
Research in Pharmaceutical Sciences |
issn |
1735-5362 1735-9414 |
publishDate |
2018-01-01 |
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. |
topic |
docking study; igf-1; igfbp-3; linker domain; molecular dynamic |
url |
http://www.rpsjournal.net/article.asp?issn=1735-5362;year=2018;volume=13;issue=4;spage=332;epage=342;aulast=Jafari |
work_keys_str_mv |
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