Modelling the Activation Pathways in Full-Length Src Kinase
Src kinases play fundamental roles in several crucial cell processes. Their activity is tightly regulated by conformational transitions between the active and the inactive forms, which are carried out by complex protein structural rearrangements. Here, we present an in-depth study of such structural...
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doaj-97bdb523b907427195f2589f5de198d72021-08-26T13:34:09ZengMDPI AGBiophysica2673-41252021-06-0111823824810.3390/biophysica1020018Modelling the Activation Pathways in Full-Length Src KinaseJosephine Alba0Maria Montagna1Marco D’Abramo2Department of Chemistry, Sapienza University of Rome, 00185 Rome, ItalyDepartment of Information Engineering, Electronics and Telecommunications, Sapienza University of Rome, 00185 Rome, ItalyDepartment of Chemistry, Sapienza University of Rome, 00185 Rome, ItalySrc kinases play fundamental roles in several crucial cell processes. Their activity is tightly regulated by conformational transitions between the active and the inactive forms, which are carried out by complex protein structural rearrangements. Here, we present an in-depth study of such structural transitions coupling extensive all-atoms molecular dynamic simulations coupled to an algorithm able to drive the system between defined conformational states. Our results, in line with the available experimental data, confirm the complexity of such a process indicating the main molecular determinants involved. Moreover, the role of an Src inhibitor—able to bind to the protein inactive state—is discussed and compared with available experimental data.https://www.mdpi.com/2673-4125/1/2/18Src kinaseactivation pathwaysmolecular dynamics |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Josephine Alba Maria Montagna Marco D’Abramo |
spellingShingle |
Josephine Alba Maria Montagna Marco D’Abramo Modelling the Activation Pathways in Full-Length Src Kinase Biophysica Src kinase activation pathways molecular dynamics |
author_facet |
Josephine Alba Maria Montagna Marco D’Abramo |
author_sort |
Josephine Alba |
title |
Modelling the Activation Pathways in Full-Length Src Kinase |
title_short |
Modelling the Activation Pathways in Full-Length Src Kinase |
title_full |
Modelling the Activation Pathways in Full-Length Src Kinase |
title_fullStr |
Modelling the Activation Pathways in Full-Length Src Kinase |
title_full_unstemmed |
Modelling the Activation Pathways in Full-Length Src Kinase |
title_sort |
modelling the activation pathways in full-length src kinase |
publisher |
MDPI AG |
series |
Biophysica |
issn |
2673-4125 |
publishDate |
2021-06-01 |
description |
Src kinases play fundamental roles in several crucial cell processes. Their activity is tightly regulated by conformational transitions between the active and the inactive forms, which are carried out by complex protein structural rearrangements. Here, we present an in-depth study of such structural transitions coupling extensive all-atoms molecular dynamic simulations coupled to an algorithm able to drive the system between defined conformational states. Our results, in line with the available experimental data, confirm the complexity of such a process indicating the main molecular determinants involved. Moreover, the role of an Src inhibitor—able to bind to the protein inactive state—is discussed and compared with available experimental data. |
topic |
Src kinase activation pathways molecular dynamics |
url |
https://www.mdpi.com/2673-4125/1/2/18 |
work_keys_str_mv |
AT josephinealba modellingtheactivationpathwaysinfulllengthsrckinase AT mariamontagna modellingtheactivationpathwaysinfulllengthsrckinase AT marcodabramo modellingtheactivationpathwaysinfulllengthsrckinase |
_version_ |
1721194727040090112 |